Too much fructose leads to weight gain & diabetes. Don't gorge on fruit.

fructose is “isocaloric but not isometabolic.” This means you can have the identical amount of calories from fructose or glucose, fructose and protein, or fructose and fat, but the metabolic effect will be entirely different.

fructose consumption leads to decreased signaling to the central nervous system from two hormones, leptin and insulin, both of which play key roles in hunger and satiety, as well as weight control.

Here’s a linked paper which gives a bit more science

Because fructose does not stimulate insulin secretion from pancreatic ß cells, the consumption of foods and beverages containing fructose produces smaller postprandial insulin excursions than does consumption of glucose-containing carbohydrate. Because leptin production is regulated by insulin responses to meals, fructose consumption also reduces circulating leptin concentrations. The combined effects of lowered circulating leptin and insulin in individuals who consume diets that are high in dietary fructose could therefore increase the likelihood of weight gain and its associated metabolic sequelae. In addition, fructose, compared with glucose, is preferentially metabolized to lipid in the liver. Fructose consumption induces insulin resistance, impaired glucose tolerance, hyperinsulinemia, hypertriacylglycerolemia, and hypertension in animal models.

high-carbohydrate meals stimulate leptin production in humans relative to high-fat meals

Diets high in fructose induce insulin resistance in rodents (87–89) and in dogs (90). For example, Thorburn et al (91) fed rats a diet containing 35% of energy as fructose for 4 wk and found reduced insulin sensitivity associated with impaired hepatic insulin action and whole-body glucose disposal. 

There are numerous studies in which dietary fructose has been shown to induce hyperlipidemia in rodents (104, 107–109). Herman et al (107) reported that rats fed a high-fructose diet had sustained elevations in serum triacylglycerol. Circulating triacylglycerol concentrations rose and remained elevated during the entire time fructose was fed (100 d) and fell promptly when a standard chow diet was instituted. The same investigators also concluded that there was a greater capacity of human liver to metabolize fructose to lipid compared with glucose because high-sucrose diets led to elevated serum triacylglycerol concentrations in humans, whereas the same amount of glucose resulted in lower concentrations of serum triacylglycerol 

Similar to insulin resistance and hyperlipidemia, many published experiments have shown that high-fructose diets induce hypertension in animals, including rodents (125–128) and dogs (90).

To put it in simpler terms…when you eat fructose alone, your blood sugar levels remain elevated. Not only that, but your liver tends to convert the fructose into fat, so the amount of in your blood gets elevated.  Not only that, but you don’t get the same feeling of fullness, so you just tend to eat more. If your there is too much fat in your bloodstream, you eventually get diabetes.

Here is an article that talks about that

a defect in insulin-stimulated glucose transport in skeletal muscle is the primary metabolic abnormality in insulin-resistant type 2 diabetics. Fatty acids appear to cause this defect in glucose transport by inhibiting insulin-stimulated tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) and IRS-1 associated phosphatidylinositol 3-kinase activity.

Here is a table, listing the amount of fructose present in various foods

Fruit Serving Size Grams of Fructose

Limes 1 medium 0

Lemons 1 medium 0.6

Cranberries 1 cup 0.7

Passion fruit 1 medium 0.9

Prune 1 medium 1.2

Apricot 1 medium 1.3

Guava 2 medium 2.2

Date (Deglet Noor style) 1 medium 2.6

Cantaloupe 1/8 of med. melon 2.8

Raspberries 1 cup 3.0

Clementine 1 medium 3.4

Kiwifruit 1 medium 3.4

Blackberries 1 cup 3.5

Star fruit 1 medium 3.6

Cherries, sweet 10 3.8

Strawberries 1 cup 3.8

Cherries, sour 1 cup 4.0

Pineapple 1 slice

(3.5” x .75”) 4.0

Grapefruit, pink or red 1/2 medium 4.3

Boysenberries 1 cup 4.6

Tangerine/mandarin orange 1 medium 4.8

Nectarine 1 medium 5.4

Peach 1 medium 5.9

Orange (navel) 1 medium 6.1

Papaya 1/2 medium 6.3

Honeydew 1/8 of med. melon 6.7

Banana 1 medium 7.1

Blueberries 1 cup 7.4

Date (Medjool) 1 medium 7.7

Apple (composite) 1 medium 9.5

Persimmon 1 medium 10.6

Watermelon 1/16 med. melon 11.3

Pear 1 medium 11.8

Raisins 1/4 cup 12.3

Grapes, seedless (green or red) 1 cup 12.4

Mango 1/2 medium 16.2

Apricots, dried 1 cup 16.4

Figs, dried 1 cup 23.0

It’s worth noting that this table is somewhat skewed. 1/16 of a water melon is 286 grams, where as a medium orange is less than half that. Who’s to say you won’t eat 1/32 of a watermelon etc.

This site, listing fructose amounts per 100g is also useful.

Agave / Agave nectar - Has a high fructose-to-glucose ratio

Aparagus  - Contains significant amounts of fructans

Apples - 6g fructose per 100g

Artichoke  - Contains significant amounts of fructans

Banana - 4.85g fructose per 100g

Blackberries - 2.4g fructose per 100g

Blueberries - 5.0g fructose per 100g

Cherries - 5.3g fructose per 100g

Currants - 3.5g fructose per 100g

Grapes - 8g fructose per 100g

Honeydew Melon - 2.9g fructose per 100g

Inulin  - Source of fructans; sometimes added to foods such as yoghurt

Kiwi fruit - 4.3g fructose per 100g

Lemon Lime soda/softdrink - 5.8g fructose per 100g

Mango - 5.5g fructose per 100g

Onion  - Contains significant amounts of fructans

Orange juice - 2.7g fructose per 100g

Oranges - 2.2g fructose per 100g

Pears - 6.2g fructose per 100g

Pineapple - 7.2g fructose per 100g

Plum - 3.0g fructose per 100g

Raisins - 30g fructose per 100g

Raspberries - 2.3g fructose per 100g

Strawberries - 2.4g fructose per 100g

Tangerines - 2.4g fructose per 100g

Watermelon - 3.35g fructose per 100g

Note that agave syrup is blamed because of its high fructose to glucose ratio, which is ironic because it’s claimed as a healthy alternative, and arguably healthier choices could be found.

Fructans is mentioned above

A fructan is a polymer of fructose molecules. They occur in foods such as agave, artichokes, asparagus, green beans, leeks, onions (including spring onions), yacon, jícama, and wheat.

Some people have trouble digesting fructose, and for those with intestinal difficulties, it is recommended that they avoid fructans.

Here’s some more about fructose malabsorption syndrome

Even in healthy persons, however, only about 25-50g of fructose per sitting can be properly absorbed. Persons with fructose malabsorption may absorb less than 25g per sitting.

This is yet another reason not to have too much fructose at once.

The article also has this table, which is interesting

Food Fructose (grams / 100 grams) Glucose (grams / 100 grams)

Sucrose (for reference) 50 50

Apples 5.9 2.4

Pears 6.2 2.8

Fruit juice e.g. Apples, Pears 5 to 7 2 to 3

Watermelon 3.4 1.6

Raisins 29.8 27.8

Honey 40.9 35.7

High fructose corn syrup 42 to 55 45 to 58

It’s not that the ratio is particularly worse in high fructose corn syrup - it’s that the quantity of sugar consumed is typically much larger than that that would be consumed when eating fruit.

If you eat small enough portions, less sugar enters your system and therefore less insulin is needed to control a blood sugar rise, and therefore less damage is done.

Let’s look at how many calories are actually burned from eating and sitting around.

A person who weighs 150 lbs. burns about 64 calories per hour while sleeping; someone who weighs 200 lbs. burns approximately 86 calories per hour while sleeping, according to Fit Watch.

Eating burns about 140 calories per hour; watching TV or reading burns around 75; and doing homework, or anything that requires heavy concentration or brain activity, burns around 110.

Let’s be generous and assume 100 calories per hour are burned. That’s 25 grams of carbohydrate. So if you were taking small nibbles or a few pieces of fruit here and there, that’s about 1.5 pieces oranges per hour, about 200 grams of orange. The calculations are similar for standard serving sizes of other fruits. Assuming there is some glucose in the fruit, for which there will be an insulin response, the amount you can eat rises somewhat.

How to make sense of the data on fructose? As I see it, each food has a functional purpose. Protein sources like steak are effective at building muscles. On the other hand if early man came upon an orchard full of fruit in the early summer, he might well gorge and it might be an evolutionary advantage for him to get fatter to take advantage of all the fruit in front of him. Now, as fruit is available in huge quantities everywhere, the possibility of getting fat from gorging on fruit is real. 

What’s the upshot? If you want to lose weight and attain better health, pay attention to the amount of fructose you consume.

If you want to improve your insulin response, consider combining fruit with protein, as protein causes insulin levels to rise, without affecting your blood sugar.

Pure protein — protein sources that do not contain any carbohydrates — do not affect your blood glucose levels

Insulin does many things at once. It causes amino acids to be taken in to cells and causes blood sugar to be lowered via a number of different mechanisms.

So, as I see it the takeaways are:

1) Avoid sugary drinks and any drinks with high fructose corn syrups (includes most sodas).

2) If you are eating a fruit that contains fructose, don’t eat too much, so as not to raise the blood sugar too high, as insulin won’t help enough. Don’t gorge on fruit. 

3) Consider eating fruit with a meal in which you have some protein.

4) Be careful with respect to the total amount of fructose you consume in any given day. The less fructose you consume the better it is for your blood sugar & the more it prevents obesity, but fruit is good for other reasons, so try to find the compromise that’s right for you.

5 out of 6 of people (or more) may have impaired health because of gluten

As Stephan highlights, one study showed that 29% of asymptomatic (read: not celiac) people nonetheless tested positive for anti-gliadin IgA in their stool. Anti-gliadin IgA is an antibody produced by the gut, and it remains there until it’s dispatched to ward off gliadin – a primary component of gluten. Basically, the only reason anti-gliadin IgA ends up in your stool is because your body sensed an impending threat – gluten. If gluten poses no threat, the anti-gliadin IgA stays in your gut. And to think, most Americans eat this stuff on a daily basis.

As the linked article says

I recently discovered the work of Dr. Kenneth Fine of EnteroLab. He has developed an assay that detects anti-gliadin IgA in stool. Gliadin is one of the problematic proteins in gluten that is implicated in gluten sensitivity. Dr. Fine has been conducting informal research using his fecal anti-gliadin IgA test (data here). He has found that:

  • 100% of untreated celiac patients are antigliadin IgA positive by fecal test, compared to only 76% by blood (n= 17).
  • 76% of microscopic colitis (a type of chronic diarrhea) patients are positive by the fecal test, compared to 9% by blood (n= 57).
  • 57% of symptomatic people (digestive problems?) are positive by the fecal test, compared to 12% by blood (n= 58).
  • 62% of people with autoimmune disease are positive by the fecal test.
  • 29% of asymptomatic (healthy) people are positive by the fecal test, compared to 11-12% by blood (n= 240).
  • Baby and cow feces are 0% positive by the stool assay.

It gets worse. Gluten sensitivity is determined in large part by genetics. A gene called HLA-DQ is intimately involved. It encodes a protein that is expressed on the surface of cells, that serves to activate immune cells when certain foreign substances are present. Different versions of the gene are activated by different substances. HLA-DQ2 and HLA-DQ8 are classically associated with celiac disease. Roughly 42% of the US population carries DQ2 or DQ8. According to Dr. Fine, every allele except DQ4 has some association with gluten-related problems! Only 0.4% of the U.S. population carries HLA-DQ4 and no other allele.
 in a preliminary study… Researchers took gut biopsies from celiac patients and asymptomatic controls. Five out of six asymptomatic controls showed elevated interleukin-15, a marker of innate immune activation, upon exposure to gliadin. An activated innate immune system (commonly called ‘inflammation’) is associated with a wide array of chronic diseases, from obesity to cancer to cardiovascular disease. Inflammatory cytokines are elevated in celiac patients and may play a role in their bone pathology. 

Megapost : First Gluten was identified. Now comes lectins, found in wheat, grains, rice, potatoes etc. Lectins can impair digestive health, mental health, cardiovascular health, and cellular function. Lectins can contribute to weight gain and diabetes, and can impair your immune system.

I continue to be interested in paleolithic diet theory. We’ve only been eating milk and grains for 10,000 years, and it takes considerably longer than that to adapt to new food groups. So it is therefore likely that we do not have the right biological structures in place to deal with those foods. As time goes by research increasingly supports this conclusion. We know that certain proteins in dairy products are linked with heart disease and poor circulation. We know that gluten can cause a plethora of problems even in those who test negative for celiac. We’re just beginning to scratch the surface when it comes to other components in other grains and dairy.

First let’s go over WGA, or wheat germ agglutinin, and the issues it brings up.

Lectin is a defense mechanism for the wheat plant, designed to ward of its natural enemies such as fungi and insects. Unfortunately, this protein is also very resistant to breakdown by living systems, and it easily accumulates in tissues where it interferes with normal biological processes and acts as an anti-nutrient.

  • Pro-Inflammatory: WGA lectin stimulates the synthesis of pro-inflammatory chemical messangers, even at very small concentrations.

  • Immunotoxic: WGA lectin may bind to and activate white blood cells.

  • Neurotoxic: WGA lectin can pass through your blood-brain barrier and may attach to the protective coating on your nerves known as the myelin sheath. It is also capable of inhibiting nerve growth factor, which is important for the growth, maintenance, and survival of certain target neurons.

  • Cytotoxic (Toxic to cells): WGA lectin may induce programmed cell death.

Further, research shows WGA lectin may even:

  • Interfere with gene expression

  • Disrupt endocrine function

  • Adversely affect gastrointestinal function

WGA lectin is capable of passing through cell membranes of your intestines, gaining entry into your body. Further, if your mucosal barrier is compromised, for instance from taking certain drugs like aspirin and ibuprofen or due to a viral or bacterial infection, lectin may become even more problematic.

Keep in mind that lectin is not only in wheat. All seeds of the grass family (rice, wheat, spelt, rye, etc.) have high levels of lectin.

Here’s more:

WGA lectin is an exceptionally tough adversary as it is formed by the same disulfide bonds that make vulcanized rubber and human hair so strong, flexible and durable. Like man-made pesticides, lectins are extremely small, resistant to break-down by living systems, and tend to accumulate and become incorporated into tissues where they interfere with normal biological processes. Indeed, WGA lectin is so powerful as an insecticide that biotech firms have used recombinant DNA technology to create genetically modified WGA-enhanced plants. 

Lectins are glycoproteins, and through thousands of years of selectively breeding wheat for increasingly larger quantities of protein, the concentration of WGA lectin has increased proportionately.

Lectins are designed “to choose” specific carbohydrates that project off the surface of cells and upon which they attach. In the case of WGA the two glycoproteins it selects for, in order of greatest affinity, are N-Acetyl Glucosamine and N-Acetylneuraminic acid (sialic acid).

All animals, including worms, fish, birds and humans, use N-Acetyglucosamine as a foundational substance for building the various tissues in their bodies, including the bones. The production of cartilage, tendons, and joints depend on the structural integrity of N-Acetylglucosamine. The mucous known as the glycocalyx, or literally, “sugar coat” is secreted in humans by the epithelial cells which line all the mucous membranes, from nasal cavities to the top to the bottom of the alimentary tube, as well as the protective and slippery lining of our blood vessels. The glycocalyx is composed largely of N-Acetylglucosamine and N-Acetylneuraminic acid (also known as sialic acid), with carbohydrate end of N-Acetylneuraminic acid of this protective glycoprotein forming the terminal sugar that is exposed to the contents of both the gut and the arterial lumen (opening).

WGA is an exceedingly small glycoprotein (36 kilodaltons)

Lectins … are notoriously dangerous even in minute doses and can be fatal when inhaled or injected directly into the bloodstream. According to the U.S. Centers for Disease Control it takes only 500 micrograms (about half a grain of sand) of ricin (a lectin extracted from castor bean casings) to kill a human.

The main source of glucosamine on the market is from the N-Acetylglucosamine rich chitin exoskelotons of crustaceans, like shrimp and crab. Glucosamine is used for reducing pain and inflammation. We do not have a dietary deficiency of the pulverized shells of dead sea critters, just as our use of NSAIDs is not caused by a deficiency of these synthetic chemicals in our diet. When we consume glucosamine supplements, the WGA, instead of binding to our tissues, binds to the pulverized chitin in the glucosamine supplements, sparing us from the full impact of WGA.

At exceedingly small concentrations (nanomolar) WGA stimulates the synthesis of pro-inflammatory chemical messengers (cytokines) includingInterleukin 1, Interleukin 6 and Interleukin 8 in intestinal and immune cells. WGA has been shown to induce NADPH-Oxidase in human neutrophils associated with the “respiratory burst” that results in the release of inflammatory free radicals called reactive oxygen species. WGA has been shown to play a causative role in patients with chronic thin gut inflammation.

WGA induces thymus atrophy in rats and may directly bind to, and activate, leukocytes. Anti-WGA antibodies in human sera have been shown to cross-react with other proteins, indicating that they may contribute to autoimmunity. Indeed, WGA appears to play a role in the pathogenesis of celiac disease (CD) that is entirely distinct from that of gluten, due to significantly higher levels of IgG and IgA antibodies against WGA found in patients with CD, when compared with patients with other intestinal disorders. These antibodies have also shown not to cross-react with gluten antigens

WGA can pass through the blood brain barrier (BBB) through a process called “adsorptive endocytosis” and is able to travel freely among the tissues of the brain which is why it is used as a marker for tracing neural circuits. WGA’s ability to pass through the BBB, pulling bound substances with it, has piqued the interest of pharmaceutical developers who are looking to find ways of delivering drugs to the brain. WGA has a unique binding affinity for N-Acetylneuraminic acid, a crucial component of neuronal membranes found in the brain, such as gangliosides which have diverse roles such as cell-to-cell contact, ion conductance, as receptors, and whose dysfunction has been implicated in neurodegenerative disorders. WGA may attach to the protective coating on the nerves known as the myelin sheath and is capable of inhibiting nerve growth factor which is important for the growth, maintenance, and survival of certain target neurons. WGA binds to N-Acetylglucosamine which is believed to function as an atypical neurotransmitter functioning in nocioceptive (pain) pathways.

WGA has been demonstrated to be cytotoxic to both normal and cancerous cell lines, capable of inducing either cell cycle arrest or programmed cell death (apoptosis).

WGA may prevent DNA replication. WGA binds to polysialic acid (involved in posttranslational modifications) and blocks chick tail bud development in embryogenesis, indicating that it may influence both genetic and epigenetic factors.

WGA has also been shown to have an insulin-mimetic action, potentially contributing to weight gain and insulin resistance

WGA induces platelet activation and aggregration. WGA has a potent, disruptive effect on platelet endothelial cell adhesion molecule-1, which plays a key role in tissue regeneration and safely removing neutrophils from our blood vessels.

WGA causes increased shedding of the intestinal brush border membrane, reduction in surface area, acceleration of cell losses and shortening of villi, via binding to the surface of the villi. WGA can mimic the effects of epidermal growth factor (EGF) at the cellular level, indicating that the crypt hyperplasia seen in celiac disease may be due to the growth-promoting effects of WGA. WGA causes cytoskeleton degradation in intestinal cells, contributing to cell death and increased turnover. WGA decreases levels of heat shock proteins in gut epithelial cells leaving these cells less well protected against the potentially harmful content of the gut lumen.

However, it makes sense to be concerned about foods other than wheat:

There are other lectins in the Western diet that have properties similar to wheat lectin (WGA), namely, “chitin-binding lectins.”  Remember, “chitins” are long polymers of n-acetyl-glucosamine, the primary binding target of wheat lectin. Wheat lectin and “chitin-binding lectin” therefore share functional similarities. 

More here

Antigenically similar chitin-binding lectins are present in the embryos of wheat, barley, and rye, members of the Triticeae tribe of the grass family (Gramineae).

Similar lectins were not detected in oats and pearl millet, members of other tribes of the Gramineae. Rice, a species only distantty related to wheat, contains a lectin that is antigenically similar to the other cereal lectins and located at the periphery of embryonic roots and throughut the coleoptile.

Tomato and potato lectins are mentioned here and here. Here is some more on tomato lectins:

Intranasal delivery of tomato lectin (LEA) elicited a strong lectin-specific systemic and mucosal antibody response but only weakly potentiated the response to co-delivered OVA. In contrast, administration of wheatgerm agglutinin (WGA) or Ulex europaeus lectin 1 (UEA-I) with OVA stimulated a serum IgG response to OVA while the lectin-specific responses (particularly for WGA) were relatively low.

However, there is some evidence tomatoes actually reduce inflammation because they also contain a number of compounds that are beneficial to health.

Of course tomatoes and the nightshade family also contain alkaloids which have negative effects on health. These amounts are clearly sufficiently low that we don’t notice it much.

Four kinds of alkaloids in the Solanaceae family include the steroid alkaloids (the alkaloid found in most nightshade foods), tropane, pyrrolizidine and indole alkaloids. Steroid alkaloids have been shown to block certain nerve activity that can, at high levels, cause muscle shaking, paralysis and respiratory difficulty. They have also been associated with inflammation, particularly in the joints. Finally, some nightshade foods like eggplant and tomato contain trace amounts of nicotine.

The essential point of the paleolithic diet is that humans didn’t discover that cooking made grains, beans, potatoes and other foods edible until 10,000 years ago. Since it takes 100,000 years to adapt to a new food group, it is likely that our bodies can not handle these foods well.

Tomatoes are actually interesting because they are in the nightshade family - the same family as potatoes. Here is some tomato history.

The Tomato History has origins traced back to the early Aztecs around 700 A.D; therefore it is believed that the tomato is native to the Americas. It was not until around the 16th century that Europeans were introduced to this fruit when the early explorers set sail to discover new lands. 

More here

Genetic evidence shows the progenitors of tomatoes were herbaceous green plants with small green fruit and a center of diversity in the highlands of Peru.

So the idea is that tomatoes are a relatively new, foreign fruit, more related to the foods that are bad for us than the foods that are good for us. The prominent members of the nightshade family are potato (except sweet potatoes and yams), tomato, eggplant, tobacco, and peppers (except black and white pepper) (includes paprika, chipotle, & cayenne).

It’s possible that we could discover that tomato lectins are not as harmful as other lectins, but I feel that given the large number of fruits out there, cutting out one is no big deal.

Tomatoes are famous for lycopene, but watermelon and papaya are also great sources there.

Source μg/g wet weight

Raw tomato 8.8–42

Watermelon 23–72

Pink grapefruit 3.6–34

Pink guava 54

Papaya 20–53

Some of the other effects of lectins are interesting to me. For example, here is a possible link between lectins and psoriasis. Of course grains have a number of anti-nutrients and while researching this, I came across benzoxazinoids, which are contained in wheat, maize, and rye, and apparently can be somewhat mutagenic.

Of course this is also an argument in favor of cutting out any type of meat that are fed grains. So the eliminates any meat that’s not grass fed. It also eliminates eggs, as almost all chickens are fed grains of some sort, even so-called pastured chickens. I thought this was interesting:

I’ve read anecdotes from celiacs who have reacted to eggs from chickens fed wheat, but not from chickens fed corn.

It is my bet that there are lot of problems associated with eggs that stem directly from the fact that modern chickens are fed wheat, soy and corn - 3 foods disallowed by the paleolithic diet. Just as meat is unhealthy, partly because of what cows are fed, in comparison to grass fed beef, my bet is eggs are not as healthy as they might be if chickens ate insects and other foods for which they were evolutionarily designed.

Coconut Oil - finding a good source and why that’s important

So as a quick intro, coconut oil is heart healthy. The saturated fatty acid in coconut oil actually raises HDL and coconut increases metabolism and makes you lose weight. Because it contains MCFAs, it’s less likely to be disturbed by cooking than olive oil. It’s probably a better health choice than olive oil - at least olive oil as it’s conventionally produced (see prior post). So as a cooking oil - like to cook eggs in for example - it might be worth a try. 

Anyway, the hard thing is finding a good source of coconut oil, which is what this post is about.

The techniques outlined in wikipedia to make coconut oil are a bit cringe-worthy, with all the bleaches and solvents added to food you actually consume. Dry processing is the standard, and it’s the worst.

Coconut oil can be extracted through “dry” or “wet” processing. Dry processing requires the meat to to be extracted from the shell and dried using fire, sunlight or kilns to create copra.[2] The copra is pressed or dissolved with solvents, producing the coconut oil and a high protein, high fiber mash. The mash is of poor quality for human consumption and is instead fed to ruminants; there is no process to extract the protein from the mash. The preparation and storage of copra often occurs in unhygienic conditions which results in a poor quality oil that requires refining before consumption. A considerable portion of the oil extracted from copra is lost due to spoilage, consumption by insects and rodents, and during the extraction process.

All “wet” process involves raw coconut rather than dried copra, using the protein in the coconut to create an emulsion of the oil and water. The more problematic step is breaking up the emulsion to recover the oil. Originally this was done through lengthy boiling, but this produces a discolored oil and is not economical; modern techniques uses centrifuges and various pre-treatments including cold, heat, acids, salts, enzymes, electrolysis, shock waves, or some combination of them. Despite numerous variations and technologies, wet processing is less viable than dry processing due to a 10-15% lower yield, even compared to the losses due to spoilage and pests with dry processing. Wet processes also requires an expensive investment of equipment and energy, incurring high capital and operating costs.[3]

Proper harvesting of the coconut (the age of a coconut can be 2 to 20 months when picked) makes a significant difference in the efficacy of the oil making process and the use of a centrifuge process makes the best final extracted product. Copra made from immature nuts is more difficult to work with and produces an inferior product with lower yields.[4]Conventional coconut oil uses hexane to extract up to 10% more oil than just using rotary mills and expellers. The oil is then refined to remove certain free fatty acids, in order to reduce susceptibility rancidification.

I’d read about the problems with coconut oil here - using the so called copra process.

Copra is dried in a wood-fuelled kiln, or in the sun, over a period of a few days. …. Copra is bulked up at an export port and shipped to a large industrial oil mill — often in Europe or Asia. Unhygienic drying, humid tropical conditions, bulk shipping and long distances, result in lengthy delays and the growth of moulds on the copra. Sometimes this leads to aflatoxin contamination. Copra oil extraction requires large-scale, high-pressure, expensive, energy-intensive equipment. Unhygienic copra means that the resultant oil is normally of low quality with a Free Fatty Acid (FFA) level of 3% or more. (FFA is one measure of rancidity of oil). Thus copra oil requires refining, bleaching and deodorising (RBD) to create a commercially acceptable product. The refining process uses hydrochloric acid, solvents and steam to strip out the contamination. Some residual solvents remain in the oil. The process also removes the natural volatiles and anti-oxidants that give pure coconut oil its unique flavour and aroma. The total process from farm to refined oil can take many months. The residual copra-meal is only suitable as animal feed but, even here, care is required because it can be contaminated with carcinogenic aflatoxin.

This company seems to have found a pretty good solution. 

“Direct Micro Expelling” is highly descriptive of the technology. It is:

• Direct — quick (oil produced within 1 hour of opening the nut) and efficient (OEE 85%)

• Micro — small scale (family farm size)

• Expelling — extraction of virgin oil and meal

The linked pdf shows a small scale organic process. It’s basically about taking out the meat, grating it, and putting it in a press. Old school. This is the kind of coconut oil you’d want to buy if you were in the market for it.

Olive Oil - more of a processed food than you think

Extra virgin olive oil is preferred because of its high phenol content. It contains:

protocatechuic acid, oleuropein, tyrosol, hydrotyrosol, dihydroxyphenylethanol, and other unique phenyl-ethyl alcohols as well as lignans and secoiridoids. 

pinoresinol and acetoxypinoresinol-are key phenol components found in extra virgin olive oil.
The high phenol concentration in extra virgin olive oil results in three key health benefits. First is the ability of this rich phenol mixture to helps protect olive oil’s vitamin E. Especially during the process of heating-and even at low heating temperatures-these phenols help to stabilize the vitamin E present in extra virgin olive oil. Second is the ability of this phenol mixture to engage in free radical scavenging. Especially when it comes to the neutralization of free radicals like hydroxyl radical and superoxide anion radical, the rich phenol mixture in extra virgin olive oil is especially important. In fact, research studies have confirmed the ability of extra virgin olive oil’s phenols to help protect against free radical damage to LDL cholesterol as well as cellular DNA.
extra virgin olive oil is able to lower certain markers of inflammation (called TXB2 and LTB2) during a window of time 2-6 hours after consumption of the extra virgin oil where olive oil from later pressings is unable to do so.

Then I read this. Olive oil fraud in Italy is fairly common with products claiming to be extra virgin that are actually not.

And this:

most commercial olive oil is processed in a manner that damages its nutritional content,  and this is only the beginning of the problems with it.

[On good small farms,] organic olives are picked by hand so as to not damage the skin or pulp. They are transported in well-aerated containers and milled within 48 hours of harvesting. Before milling, leaves and twigs are removed; the olives are washed, dried, and then crushed. The oil is separated from the olive paste without the use of heat, hot water, or solvents, and it is left unfiltered, as filtering also removes many nutrients. The first pressing produces the best extra virgin oil.

[In modern factories] olives are machine harvested along with leaves and twigs. Olives that have dropped on the ground are often mixed with the good ones. They are shipped in all kinds of containers, many of which are poorly ventilated, and heaped in large piles. (Here, olives are stored for too long and often become moldy.) The oil is then extracted in a continuous centrifuge while hot water is used to help separate out the oil. Antioxidant polyphenols are soluble in water and are washed away in this process, thereby lowering the shelf life and the nutritional quality of the oil. Italy alone produces 800,000 cubic meters of waste water per year from this process. Because substantial amounts of antioxidants are washed away, factory produced olive oil has a short shelf life of only months, whereas real olive oil lasts for two to three years.

the term “extra virgin” has no official meaning in the United States. The U.S. is not a member of the International Olive Oil Council. So olive oil sold here can be labeled “extra virgin” without meeting the accepted international standards. …

Investigators have gathered evidence indicating that the biggest olive oil brands in Italy, Bertolli, Sasso, and Cirio, have for years been systematically diluting their extra virgin olive oil with cheap, highly- refined hazelnut oil imported from Turkey. Despite the fact that details of this scandal have been published in Merum, a Swiss-German magazine, and in Italian journals such as Agra Trade, and the newspaper Gazzetta del Mezzogiorno, this information has been successfully suppressed and is known to only a handful of people. International arrest warrants have been issued and seized documents indicate that at least 10,000 tons of hazelnut oil is involved. As much as 20% refined hazelnut oil can be added to olive oil and still be undetectable to the consumer.

In 1996, a study by the FDA found that 96% of the olive oils they tested, while being labeled 100% olive oil, had been diluted with other oils. A recent study in Italy found that only 40% of the olive oil brands labeled “extra virgin” actually met those standards.

Italy produces 400,000 tons of olive oil for domestic consumption, but 750,000 tons are sold. The difference is made up with highly refined, nut and seed oils. Less strict guidelines make the situation even worse in the United States. Like in Italy, more oil is “produced” in California than there are olives available. The difference is made up with less expensive oils such as corn, soy, and sunflower. The problem is these other oils have been refined. The high temperatures of the refining process change the molecular structure of the oils, making them toxic.

Apparently you can eat raw, unsalted olives, but they are hard to find.

I’ve talked to some people who have been to Italy and Spain and say the olive oil there can actually be green in color because if it’s made naturally and not processed, and that it tastes so much better made by hand.

What’s the upshot? First I think you have to look at the ingredients on your olive oil. Second, olive oil is not as healthy as you think, and you might be better off with avocados or some other form of healthy fat.

In terms of a cooking oil, there are alternatives, and I’ll do a post on that later. Of course I would be interested to buy olive oils that are made in a way that is more health conscious, and I’ll post if I find something like that.

More on working while standing up

NYT, 2010:

it looks as though there’s a more sinister aspect to sitting, too. Several strands of evidence suggest that there’s a “physiology of inactivity”: that when you spend long periods sitting, your body actually does things that are bad for you. As an example, consider lipoprotein lipase. This is a molecule that plays a central role in how the body processes fats; it’s produced by many tissues, including muscles. Low levels of lipoprotein lipase are associated with a variety of health problems, including heart disease. Studies in rats show that leg muscles only produce this molecule when they are actively being flexed (for example, when the animal is standing up and ambling about). The implication is that when you sit, a crucial part of your metabolism slows down. Nor is lipoprotein lipase the only molecule affected by muscular inactivity. Actively contracting muscles produce a whole suite of substances that have a beneficial effect on how the body uses and stores sugars and fats.

This article adds:

One study found that a woman’s risk of developing metabolic syndrome increased 26% for every extra hour of sitting. Prolonged sitting in an upright position can place strain on the back resulting in chronic pain. Blood clots are another risk of being inactive.

This adds:

The chair is a bit like wheat, actually: a relative novelty to which we aren’t physiologically adapted that has become a cultural staple nonetheless. 

Acutely, sitting weakens our muscles, especially in the legs and the hips. When you sit, your glutes are totally inactive. They aren’t being used. They’re stretched out. It’s just one big static stretch, all day long, which weakens them. Strong, engaged glutes are required for effective, natural movement. Running, walking, lifting weights – if you’re doing any of this with weak, inactive glutes from excessive sitting, you’re an injury waiting to happen. Sitting also causes permanent hip flexion. It shortens your hip flexors and makes them tight. Without good hip mobility and strength, your ability to perform the compound lower body lifts, let alone just walk around and perform day-to-day motions, is going to be severely compromised.

Treehugger adds:

Standing in one place is hard work. To stand, you have to tense your leg muscles, and engage the muscles of your back and shoulders; while standing, you often shift from leg to leg. All of this burns energy.

The Canadian Centre for Occupational Health and Safety suggests that working in a standing position can cause health problems of its own.

Working in a standing position on a regular basis can cause sore feet, swelling of the legs, varicose veins, general muscular fatigue, low back pain, stiffness in the neck and shoulders, and other health problems. These are common complaints among sales people, machine operators, assembly-line workers and others whose jobs require prolonged standing.

But most knowledge workers don’t have to stand in one position all day. Jamis at 37 Signals says it gives him greater clarity of thought.

I noticed an immediate increase in my ability to focus on a problem for longer, and with greater clarity. When I was blocked by some problem, I was able to just walk away from the desk, whereas before the effort of getting up from my chair often made me prefer to just sit and stew in my frustration.

I have to wonder if variety is the way to go - sometimes work sitting, sometimes standing.

You actually can get large muscles from lifting light weights. Here’s how:

It turns out that lifting a weight that’s 90% of the maximum weight you can lift until you can’t lift any more (failure) is less effective at muscle building than lifting a weight that’s 30% of the maximum weight you can lift until you can’t life any more (failure). It turns out you lift the lighter weight a lot more times and that builds more muscle. here is that study: via

We report for the first time that low-load high volume resistance exercise (30FAIL) is more effective at increasing muscle protein synthesis than high-load low volume resistance exercise (90FAIL). Specifically, the 30FAIL protocol induced similar increases in MYO protein synthesis to that induced by the 90FAIL protocol at 4 h post-exercise but this response was sustained at 24 h only in 30FAIL. …  There were three groups: 90% 1RM to failure (90FAIL), 30% 1RM which matched the external work to the 90FAIL group (30WM), and 30% 1RM to failure (30FAIL). 

The fact is that most people when lifting a light weight don’t lift it enough times to reach failure, so that’s probably why this study is a bit counter intuitive.
The reality is if you push yourself to near failure any weight and rep combination, you’ll likely get results.

Is Sitting a Lethal Activity? - NYTimes.com

Why do some people who consume the same amount of food as others gain more weight? After assessing how much food each of his subjects needed to maintain their current weight, Dr. Levine then began to ply them with an extra 1,000 calories per day. Sure enough, some of his subjects packed on the pounds, while others gained little to no weight.

Then six years later, with the help of the motion-tracking underwear, they discovered the answer. “The people who didn’t gain weight were unconsciously moving around more,” Dr. Jensen says. They hadn’t started exercising more — that was prohibited by the study. Their bodies simply responded naturally by making more little movements than they had before the overfeeding began, like taking the stairs, trotting down the hall to the office water cooler, bustling about with chores at home or simply fidgeting. On average, the subjects who gained weight sat two hours more per day than those who hadn’t.

The conventional wisdom, though, is that if you watch your dietand get aerobic exercise at least a few times a week, you’ll effectively offset your sedentary time. A growing body of inactivity research, however, suggests that this advice makes scarcely more sense than the notion that you could counter a pack-a-day smoking habit by jogging.

This is your body on chairs: Electrical activity in the muscles drops — “the muscles go as silent as those of a dead horse,” Hamilton says — leading to a cascade of harmful metabolic effects. Your calorie-burning rate immediately plunges to about one per minute, a third of what it would be if you got up and walked. Insulin effectiveness drops within a single day, and the risk of developing Type 2 diabetesrises. So does the risk of being obese. The enzymes responsible for breaking down lipidsand triglycerides — for “vacuuming up fat out of the bloodstream,” as Hamilton puts it — plunge, which in turn causes the levels of good (HDL) cholesterol to fall.

In studies of rats who were forced to be inactive, for example, he discovered that the leg muscles responsible for standing almost immediately lost more than 75 percent of their ability to remove harmful lipo-proteins from the blood. 

 To show that the ill effects of sitting could have a rapid onset in humans too, Hamilton recruited 14 young, fit and thin volunteers and recorded a 40 percent reduction in insulin’s ability to uptake glucose in the subjects — after 24 hours of being sedentary.

Alpa Patel, an epidemiologist at the American Cancer Society, tracked the health of 123,000 Americans between 1992 and 2006. The men in the study who spent six hours or more per day of their leisure time sitting had an overall death rate that was about 20 percent higher than the men who sat for three hours or less. 

Alpa Patel, an epidemiologist at the American Cancer Society, tracked the health of 123,000 Americans between 1992 and 2006. The men in the study who spent six hours or more per day of their leisure time sitting had an overall death rate that was about 20 percent higher than the men who sat for three hours or less. The death rate for women who sat for more than six hours a day was about 40 percent higher. Patel estimates that on average, people who sit too much shave a few years off of their lives.

Another study, published last year in the journal Circulation, looked at nearly 9,000 Australians and found that for each additional hour of television a person sat and watched per day, the risk of dying rose by 11 percent. The study author David Dunstan wanted to analyze whether the people who sat watching television had other unhealthful habits that caused them to die sooner. But after crunching the numbers, he reported that “age, sex, education, smoking, hypertension, waist circumference, body-mass index, glucose tolerance status and leisure-time exercise did not significantly modify the associations between television viewing and all-cause … mortality.”

Dr. Levine knows that we can’t all be farmers, so instead he is exploring ways for people to redesign their environments so that they encourage more movement. We visited a chairless first-grade classroom where the students spent part of each day crawling along mats labeled with vocabulary words and jumping between platforms while reciting math problems. We stopped by a human-resources staffing agency where many of the employees worked on the move at treadmill desks — a creation of Dr. Levine’s, later sold by a company called Steelcase.

brilliant article :)

Sprints and Youthfulness - Exploring the connection - and how to start sprint training to reap the benefits - weight lifting tie in

So I came across this article

“Leukocyte Telomere Length is Preserved with Aging in Endurance Exercise-Trained Adults and Related to Maximal Aerobic Capacity” via @mercola.

OK, this is really cool - and interesting for anyone interested in fitness.

OK, so normally as you get older, your telomeres shorten and that causes a whole lot of aging related problems.

This is a small study, but it shows that telomere length is preserved - if you among those who do endurance exercise… and it’s related to your so-called VO2 max - which is basically an estimate of the most oxygen you can consume during exercise…it’s a measure of how hard you can push yourself doing a sprint in any number of different types of exercises.

This is interesting because a number of studies have demonstrated that doing short sprints is actually more effective than aerobic workouts in terms of cardiovascular benefits.

To me, this is an additional, important data point, that if you care about fitness, and you devote time to stay in shape, you really owe it to yourself to do some sort of sprint - it doesn’t matter whether you’re sprinting up stairs or running your fastest - it’s about getting your heart, lungs, body, and body overall to go as fast as it can.

Here’s how runner’s world puts it :

Consistent aerobic conditioning will increase your max, but only by so much. French exercise physiologist Veronique Billat found that the fastest way to reach your potential is to run intervals at a speed that elicits your VO2 max, a pace known in lab circles as velocity. 

I suspect that improved cardiovascular fitness is directly tied to mental acuity and mood, and to me this is one very important molecular marker that sprints are quite important.

So the next question is if you’re going to start doing sprints at a gym or on a track, how should you go about it? Wikipedia calls sprint training HIIT (High Intensity Interval Training):

Usual HIIT sessions may vary from 9–20 minutes. The original protocol set a 2:1 ratio for work to recovery periods. For example, a runner would alternate 15–20 seconds of hard sprinting with 10 seconds of jogging or walking.

A HIIT session consists of a warm up period of exercise, followed by six to ten repetitions of high intensity exercise, separated by medium intensity exercise, and ending with a period of cool down exercise. The high intensity exercise should be done at near maximum intensity. The medium exercise should be about 50% intensity. The number of repetitions and length of each depends on the exercise. The goal is to do at least six cycles, and to have the entire HIIT session last at least fifteen minutes and not more than twenty.

A study by Gibala et al.[5] demonstrated 2.5 hours of sprint interval training produced similar biochemical muscle changes to 10.5 hours of endurance training and similar endurance performance benefits. 

A recent study by Driller[11] showed an 8.2 second improvement in 2000m rowing time following 4 weeks of HIIT in well-trained rowers. The interval training used by Driller and colleagues involved 8 x 2.5 minute work bouts at 90% of VO2max, with individualized recovery intervals between each work bout

Recently it has been shown that two weeks of HIIT can substantially improve insulin action in young healthy men.[12] HIIT may therefore represent a viable method for prevention of type-2 diabetes.

So, if those are the basic parameters, what is optimal? As this site says,

elite athletes cannot sustain an all-out effort for more than 60 seconds, which means the average exerciser’s full speed limitations are probably closer to 15-30 seconds. 

If the goal is to be able to increase your sprinting ability - and improve the lengths of your sprints, it seems to me that sprinting intervals should be as close to your max as possible for as long as you can sustain that maximum. The rest interval would be about half of that amount, but can vary.

As this article suggests, there may be other reasons to keep your sprint short. 

Studies also show that shorter intervals don’t feel as physically demanding as long intervals — so you can get better results without feeling like you’re working harder.

The article mentions myoglobin which holds oxygen, which is used to burn fat during fast sprints. 

Myoglobin holds enough oxygen to last for 5-15 seconds [Astrand, I., & Astrand, P-O. (1960). Myohemoglobin as an oxygen-store in man. Acta Physiologica Scandinavica, 48, 454-460]

myoglobin is repeatedly used and reloaded during the work and recovery phases of interval exercise.

This is another reason why an all out sprint is limited in terms of time.

Interestingly this may also be related to how weight lifters typically limit their number of repetitions to about 8 reps. That’s the maximum “sprint” that a muscle can maintain. In this view point, myoglobin could almost be view as the lungs of the muscle, and that you are partly working to improve the respirative ability of muscles. In my view this is likely one reason why shorter sets work for muscular development. However it also suggests to me that some may be able to sustain a longer “sprint” and that may be effective, provided they work towards muscle exhaustion. Indeed other studies have shown that as long as the muscle reaches failure - or comes close, lower weights and higher reps may have more benefits. It just takes a lot longer to reach failure with lower weights.

So, with sprints the idea is that doing sprint training for 20 minutes provides the cardiovascular benefits of lifting a lower weight for much longer. Similarly with weight training doing 3 sets or sprints to failure provides the benefits of a much longer workout.

Indeed people who train for power lifting (low rep, high weight), also have longer telomeres than age matched controls.

As see it, any type of sprint, whether it’s on a track, on a rowing machine or stair climber, or on a set with heavy weight spurs more rapid gains in terms of growth in fitness than so called endurance workouts, and it appears they help make you more youthful as well. Telomeres are just a marker, so my guess is that those who sprint and lift have better skin, more energy etc. than people of a similar age who do not do those same activities. 

Milk - not doing a body good. Exploring the connection with stress, histamine, heart disease, diabetes, autism/asd, schizophrenia, more…

Milk is a sedative:

For generations, mothers have given their children a warm glass of milk before bed as a way to help them fall asleep. As far back as 1934, this home remedy gained scientific validation when it was observed that people who ate milk and cornflakes were more likely to enjoy a full night of uninterrupted sleep.

In 1997, pediatric researchers added to the evidence by demonstrating that newborns given an infant formula containing milk fell asleep not solely due to nursing and being held, but owing specifically to something in milk itself.

In 2000, researchers identified what that “something” was. It turns out that nutrients found in cow’s milk called bioactive peptides (chains of amino acids) exert a sedative effect on the brain and induce sustained sleep patterns.

These bioactive milk peptides have since been shown to act on the brain’s GABA-A receptors, the same mechanism of action that makes the class of sedatives known as benzodiazepines so effective. The advantage of milk peptides, of course, is that they induce relaxation and sleep without the side effects associated with long-term benzodiazepine use.

In pre-clinical models, milk peptides markedly reduce anxiety and improve sleep in animals subjected to chronic stress.

In human studies, a proprietary bioactive milk peptide compound used widely in Europe has been shown to effectively induce relaxation, leading not only to deeper, more restorative sleep, but also to substantial improvements across a wide range of stress markers.

The article cited above goes on to talk about how their milk extract is marvelous, and how it succeeds in reducing stress in additional clinical trials.

Milk contains casein…

Casein has been documented to break down in the stomach to produce the peptide casomorphin, an opioid that acts as a histamine releaser. 

What are the effects of this histamine release?. It’s complicated because there are multiple receptors for it:H1,H2,H3,H4, each of which do something different when histamine is released and stimulates them:

  • [H1] Histamine heightens allergic reactions and those you experience during colds and allergies. It makes you more likely to cough and sneeze. On your skin it makes you more likely to have eczema and get hives and it makes insect bites more itchy. For your stomach, it heightens nausea and motion sickness. It also wakes the body up, perhaps to deal with these perceived problems.
  • [H2] Histamine dilates your blood vessels, and is involved in erections. It also inhibits part of your immune system (antibody synthesis, T-cell proliferation and cytokine production).
  • [H3] Makes you sleepy and lessens pain perception. So H1 makes you awake, but H3 makes you sleep, so for whatever reason milk’s action on the H3 histamine receptors appear to override its effects on H1 receptors. 
  • [H4] Active in bone marrow and the immune system.

So how to make sense of these different ways in which Histamine acts? As this site says,

Histamine is an immune system mediator or, more simply, a chemical messenger that helps direct your body’s response to a foreign invader. 

It essentially tells your body, get overly active in fighting off a perceived acute disease or threat of some sort - and get a little bit stressed out about it - and lower general immunity, relax with respect anything other than this acute problem, and go to sleep.

So histamine takes a small issue - whether it’s bee pollen or some other allergen, and makes your body perceive it to be a huge problem and totally focuses your body on defending itself from said problem. My guess is it does the same thing in your brain personality-wise. It makes you more likely to recognize something small as a major acute problem which must be dealt with immediately. In the absence of a perceived stress - which would probably be amplified by the histamine - it is likely sedative.

Milk is bad in other ways….

Milk contains a small amount of actual morphine - which in itself is interesting.

Casein breaks down down into a few things in your gut, one of which is BCM-7.

BCM-7 has been implicated in the development of both ischaemic heart disease (IHD)  and diabetes mellitus type I (DM-I) (Elliott et al. 1999; Thorsdottir et al. 2000; McLachlan 2001; Laugesen and Elliott 2003; Tailford et al. 2003)

For IHD, BCM-7 could act on LDL through peroxidation of the lipids within LDL  through a tyrosyl radical mechanism of action (Elliott at al. 1999; Heinecke et al. 1999).

For DM-I…BCM-7 suppresses immune defense mechanisms by inhibiting the incorporation of thymidine into lymphocyte DNA replication thereby inhibiting lymphocyte proliferation (Elitsur and Luk 1991). This generates an immune vulnerability (in the case of DMI) to a certain class of enteroviruses that are still being researched as they may have potential key roles in the damage done to pancreatic beta cells (Graves et al. 1997). Through BCM-7 compromising the immune system, the system is more vulnerable to all kinds of pathogenic infections. 

 BCM-7 acts on the mu-opioid receptor which in turn causes the release of histamine (Kostyra et al. 2004)

The suspected heart disease and diabetes mechanism has everything to do with the protein in milk (Casein which breaks down into BCM-7) and little to do with the saturated fat in the milk. More on that correlation.

Milk causes a release of intestinal mucous.

Like heroin or codeine, casomorphins slow intestinal movements and have a decided antidiarrheal effect. The opiate effect may be why adults often find that cheese can be constipating, just as opiate painkillers are.

More on that release of intestinal mucous.

There is some evidence that casein and gluten (a milk protein) worsen autism, and move you along the autistic scale.

More on autism and heart disease/diabetes:

Studies involving large samples of  patients with autism, schizophrenia, or mania found that over 90 % of those tested had high levels of the milk protein beta-casomorphine-7 in their blood and urine and defective enzymatic processes for digesting milk protein(24,25,27), and similarly for the corresponding enzyme needed to digest wheat gluten(24,26). Like casein, gluten breaks down into molecules with opioid traits, called gluteomorphine or gliadin. As with caseomorphin, it too can retain biological activity if the enzymes needed to digest it are not functioning properly..

In hydrolysed milk with variant A1 of beta-casein, BCM-7 level is 4-fold higher than in A2 milk.  Variants A1 and A2 of beta-casein are common among many dairy cattle breeds. A1 is the most frequent in Holstein-Friesian (0.310–0.660), Ayrshire (0.432–0.720) and Red (0.710) cattle. In contrast, a high frequency of A2 is observed in Guernsey (0.880–0.970) and Jersey (0.490–0.721) cattle(92). In children with autism, most of whom have been found to have been exposed to high levels of toxic metals through vaccines, mother’s dental amalgams, or other sources;   higher levels ofBCM-7 is found in the blood(24-26). 

Epidemiological evidence from New Zealand claims that consumption of beta-casein A1 is associated with higher national mortality rates from ischaemic heart disease. It appears that the populations that consume milk containing high levels of beta-casein A2 have a lower incidence of cardiovascular disease and type 1 diabetes. 

A double blind study using a potent opiate antagonist, naltrexone (NAL), produced significant reduction in autistic symptomology among the 56% most responsive to opioid effects(28). 

Of course you’ll get less heart disease in a population that drinks a form of milk with less beta-casein, but of course one might postulate that heart disease would be further reduced with casein and milk elimination.