18 replies to this topic

[chrisp2]

What do you guys think about casein?

Reading some posts here (by searching) there is some mention of it interfering with polyphenols in tea... And some indication of it being indicated with cancer.

But I didn't really see a lot on the boards about how seriously one should be concerned with reducing or eliminating casein?

I ask because it seems to be the only protein source that you can take and it will very slowly - over a period of up to 8 hours.

[eldar]

I ask because it seems to be the only protein source that you can take and it will very slowly - over a period of up to 8 hours.

If you are worried use egg protein instead. It's pretty much a perfect protein source.

[chrisp2]

I think casein proteins are the only ones that will remain in the stomach for any significant amount of time.

I read elsewhere that only casein is released over a long period of time from your stomach to small intestines. The statement is that other proteins are released into the small intestine, and if they are not absorbed within a reasonable amount of time, they become useless. (I assume the point is that the proteins only have a certain amount of time to be absorbed in the small intestine before pushing further on down... While casein slowly enters the intestines and therefore will be fully digested)

[EmbraceUnity]

I am concerned about it too, but most studies I have seen are contradictory or inconclusive. Milk is a big industry, so that almost certainly has something to do with it.

My health, as far as I can tell, is in optimal condition and I have decent muscle mass. For my protein I mostly rely on eggs, nuts, salmon, and poultry. I don't use any whey supplements. For health reasons, I take lactoferrin and buy a brand of milk that is organic, grass-fed, and vat pasteurized. To be safe, I try to avoid having milk too soon after consuming antioxidants.

There is an equal amount of controversy with soy, so I don't use soy supplements. I only drink soy milk occasionally as a substitute if I have consumed antioxidants within the past hour.

[chrisp2]

Yes - I too stay away from soy. Too much controversy.

Although I see little such controversy with Whey. Almost everything that is published seems to say good thing s about it.

[eldar]

I  think casein proteins are the only ones that will remain in the stomach for any significant amount of time.

I am pretty confident that this is not the case. Any studies to back this up?

Whey protein gets digested really fast so that is not something you want to take at night.
Other than that egg protein, meat, fish and chicken are very good to take for a slower digested protein.

And as far as I know there is little to none controversy regarding egg protein.

[neogenic]

Casein is the slowest to release, especially micellar casein. It seems odd to assume a milk protein that is much like that given to all mammals to maintain life is getting put down over animal flesh or embryos. Certainly soy is steeped in controversy and the only pro-side is supported by the industry. Affecting the endrinological cascade can have drastic impact, especially on the hypogonadal, pubescent, and infant/toddlers. Certainly cow's milk can be a negative for infants due to osmolarity and mineral content differences and their undeveloped gut...leading to diarrhea.

Whey and casein have so many positive studies. There is genius (in God) to make a fast and slow protein combined. Rapid acting and long acting. As far as anti catabolic/anabolic/nitrogen retention its unsurpassed.

A New study showing the benefit of Whey/Casein/Calcium:
: Br J Nutr. 2007 Aug 13;:1-8 [Epub ahead of print] Links
High-calcium diet with whey protein attenuates body-weight gain in high-fat-fed C57Bl/6J mice.Pilvi TK, Korpela R, Huttunen M, Vapaatalo H, Mervaala EM.
Foundation for Nutrition Research, PO Box 30, FIN-00390 Helsinki, Finland.

An inverse relationship between Ca intake and BMI has been found in several studies. It has been suggested that Ca affects adipocyte metabolism via suppressing 1,25-dihydroxycholecalciferol (1,25(OH)2-D3) and decreases fat absorption. We studied the effect of Ca and milk proteins (whey and casein) on body weight in C57Bl/6J mice. Male mice, age 9 weeks, were divided into three groups (ten mice per group) receiving modified high-fat (60 % of energy) diets. Two groups received a high-Ca diet (1.8 % calcium carbonate (CaCO3)), with casein or whey protein (18 % of energy), and one group received a low-Ca diet (0.4 % CaCO3) with casein for 21 weeks. Food intake was measured daily and body weight twice per week. Body fat content (by dual-energy X-ray absorptiometry) of all mice and faecal Ca and fat excretion of seven mice/group were measured twice during the study. Final body weight (44.1 (sem 1.1) g) and body fat content (41.6 (sem 0.6) %) were significantly lower (P < 0.05) in the high-Ca whey group than in the low-Ca casein group (48.1 (sem 0.8) g and 44.9 (sem 0.8) %). Body weight and body fat content of the high-Ca casein group did not differ significantly from the low-Ca casein group even though serum 1,25(OH)2-D3 levels were significantly lower (P < 0.001) in both high-Ca groups than in the low-Ca casein group. Thus changes in serum 1,25(OH)2-D3 do not seem to affect body weight in this animal model. There was a significant difference in fat excretion between the high-Ca whey and low-Ca casein groups (3.9 (sem 0.9) % in the high-Ca whey v. 1.4 (sem 0.2) % in the low-Ca casein group; P < 0.05), which may partly explain the effect on body weight.

How about a full breakdown all all of milk's components from a reivew:
J Exp Ther Oncol. 2007;6(2):89-106.Links
Milk-derived proteins and peptides of potential therapeutic and nutritive value.Zimecki M, Kruzel ML.
Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wroclaw, Poland.

Milk and colostrum are rich in proteins and peptides which play a crucial role in development of the immune system in mammalian offspring. Immunotropic properties of these compounds prompted investigators to search for their utility in prevention and therapy of various disorders in humans. The following constituents of milk are of particular interest: 1) Lactoferrin (LF)--exhibits antibacterial, antifungal, antiviral, antiparasite and antitumor activities. It is protective with regard to intestinal epithelium, promotes bone growth and accelerates recovery of the immune system function in immunocompromised animal; 2) A Proline-Rich Polypeptide (PRP) shows a variety of immunotropic functions, including promotion of T-cell maturation and inhibition'of autoimmune disorders. PRP was recently found to improve or stabilize the Instrumental Activity of Daily Living status in Alzheimer's disease patients. 3) Casein--has been protective in experimental bacteremia by eliciting myelopoiesis. Casein hydrolyzates were also protective in diabetic animals, reduced the tumor growth and diminished colicky symptoms in infants. Casein-derived peptides have been found to have antihypertensive effects. Glycomacropeptide (GMP)--a peptide derived from kappa casein, exhibits antibacterial and antithrombotic activities. 4) Alpha lactalbumin (LA)--demonstrates antiviral, antitumor and anti-stress properties. LA-enriched diets were anxiolytic, lowered blood pressure in rats, prevented diarrhea and led to a better weight gain in malnourished children. 5) Lysozyme--is effective in treatment of periodentitis and prevention of tooth decay. Milk enriched in lysozyme was used in feeding premature infants suffering from concomitant diseases. 6) Lactoperoxidase--shows antibacterial properties. In conclusion, milk-derived proteins and peptides are bio-accessible and safe for the prevention and treatment of numerous disorders in humans.

[neogenic]

a study in 2003 came out stating there was a weak correelation of beta-casein to atherogenesis...later that year they released:
Atherosclerosis. 2003 Sep;170(1):11-2. Links
Comment on:
Atherosclerosis. 2003 Sep;170(1):13-9.
Beta-casein variants and atherosclerosis-claims are premature.

In 2006:
Atherosclerosis. 2006 Sep;188(1):175-8. Epub 2005 Nov 18. Links
A comparison of the effects of A1 and A2 beta-casein protein variants on blood cholesterol concentrations in New Zealand adults.Venn BJ, Skeaff CM, Brown R, Mann JI, Green TJ.
Department of Human Nutrition, University of Otago, P.O. Box 56, Dunedin, New Zealand.

Beta-casein is a cow's milk protein that occurs predominantly in two forms, A1 and A2. Epidemiological evidence suggests that per capita consumption of beta-casein A1 is associated with national mortality rates from ischaemic heart disease. A biological mechanism was proposed after rabbits fed diets containing beta-casein A2 had lower serum cholesterol concentrations and less aortic intimal thickening than rabbits fed beta-casein A1. We tested whether beta-casein A1 and A2 variants differentially affect plasma cholesterol concentrations in humans. In a randomised crossover trial of two four-and-a-half week periods without washout, 62 participants replaced all dairy products in their diet with 500 mL of low-fat milk and 28 g of full-fat cheese that differed in the proportion of beta-casein A1 and A2 variants. Duplicate blood samples were taken on non-consecutive days at the end of each treatment period from 55 people who completed the study. Mean (S.D.) plasma total, low-density and high-density lipoprotein cholesterol concentrations were 5.60 (0.77), 3.73 (0.70) and 1.26 (0.34) mmol/L after the A1 diet and 5.63 (0.81), 3.75 (0.75) and 1.27 (0.37) mmol/L after the A2 diets. We found no evidence that dairy products containing beta-casein A1 or A2 exerted differential effects (P > 0.05) on plasma cholesterol concentrations in humans.

I've flipped through 10-15 studies from the peer-reviewed journals and they state no eefect on cholesterol, atherogenesis, lipoproteins, there are studies with growth/development (positive), reversing tumor growth, reduction of diabetic symptoms, improved immune function, and increased bone mineral density.

I found studies with rats (above with humans) that showed reduction of inflammtion via TGF-beta.

Here's a study showing the synergy of milk proteins:

Am J Clin Nutr. 2006 Nov;84(5):1070-9. Links
Comment in:
Am J Clin Nutr. 2007 Jun;85(6):1664; author reply 1664-5.
Compared with casein or total milk protein, digestion of milk soluble proteins is too rapid to sustain the anabolic postprandial amino acid requirement.Lacroix M, Bos C, Léonil J, Airinei G, Luengo C, Daré S, Benamouzig R, Fouillet H, Fauquant J, Tomé D, Gaudichon C.
UMR INRA 914, Physiology of Nutrition and Feeding Control Unit, Institut National Agronomique Paris-Grignon, Paris, France.

BACKGROUND: The in vivo quality of milk protein fractions has seldom been studied in humans. OBJECTIVE: Our objective was to compare the postprandial utilization of dietary nitrogen from 3 [(15)N]-labeled milk products: micellar caseins (MC), milk soluble protein isolate (MSPI), and total milk protein (TMP). DESIGN: The macronutrient intakes of 23 healthy volunteers were standardized for 1 wk, after which time the subjects ingested a meal containing MC (n = 8), MSPI (n = 7), or TMP (n = 8). [(15)N] was measured for an 8-h period in plasma amino acids, proteins, and urea and in urinary urea. RESULTS: The transfer of dietary nitrogen to urea occurred earlier after MSPI ingestion than after MC and TMP ingestion, and concentrations remained high for 8 h, concomitantly with higher but transient hyperaminoacidemia and a higher incorporation of dietary nitrogen into plasma amino acids. In contrast, deamination, postprandial hyperaminoacidemia, and the incorporation of dietary nitrogen into plasma amino acids were lower in the MC and TMP groups. Finally, total postprandial deamination values were 18.5 +/- 2.9%, 21.1 +/- 2.8%, and 28.2 +/- 2.9% of ingested nitrogen in the TMP, MC, and MSPI groups, respectively. CONCLUSIONS: Our results confirm the major role of kinetics in dietary nitrogen postprandial utilization and highlight the paradox of MSPI, which, despite its high Protein Digestibility Corrected Amino Acid Score, ensures a rate of amino acid delivery that is too rapid to sustain the anabolic requirement during the postprandial period. Milk proteins had the best nutritional quality, which suggested a synergistic effect between soluble proteins and caseins.

PMID: 17093159 [PubMed - indexed for MEDLINE

And for bodybuilding/weight training:

1: Med Sci Sports Exerc. 2004 Dec;36(12):2073-81. Links
Ingestion of casein and whey proteins result in muscle anabolism after resistance exercise.Tipton KD, Elliott TA, Cree MG, Wolf SE, Sanford AP, Wolfe RR.
Metabolism Unit, Shriners Hospitals for Children and Department of Surgery, The University of Texas Medical Branch, Galveston, TX 77550, USA. ktipton@utmb.edu

PURPOSE: Determination of the anabolic response to exercise and nutrition is important for individuals who may benefit from increased muscle mass. Intake of free amino acids after resistance exercise stimulates net muscle protein synthesis. The response of muscle protein balance to intact protein ingestion after exercise has not been studied. This study was designed to examine the acute response of muscle protein balance to ingestion of two different intact proteins after resistance exercise. METHODS: Healthy volunteers were randomly assigned to one of three groups. Each group consumed one of three drinks: placebo (PL; N = 7), 20 g of casein (CS; N = 7), or whey proteins (WH; N = 9). Volunteers consumed the drink 1 h after the conclusion of a leg extension exercise bout. Leucine and phenylalanine concentrations were measured in femoral arteriovenous samples to determine balance across the leg. RESULTS: Arterial amino acid concentrations were elevated by protein ingestion, but the pattern of appearance was different for CS and WH. Net amino acid balance switched from negative to positive after ingestion of both proteins. Peak leucine net balance over time was greater for WH (347 +/- 50 nmol.min(-1).100 mL(-1) leg) than CS (133 +/- 45 nmol.min(-1).100 mL(-1) leg), but peak phenylalanine balance was similar for CS and WH. Ingestion of both CS and WH stimulated a significantly larger net phenylalanine uptake after resistance exercise, compared with the PL (PL -5 +/- 15 mg, CS 84 +/- 10 mg, WH 62 +/- 18 mg). Amino acid uptake relative to amount ingested was similar for both CS and WH (approximately 10-15%). CONCLUSIONS: Acute ingestion of both WH and CS after exercise resulted in similar increases in muscle protein net balance, resulting in net muscle protein synthesis despite different patterns of blood amino acid responses.

PMID: 15570142 [PubMed

I've personally spoke to some of these men about this study and they've done more research since. I believe in whey/ casein.

My ultimate protein is whey isolate and micellar casein 50/50. Xtreme Formulations is a company that does this pre-flavored/pre-done. True Protein and Protein Factory could do this as well.

[eldar]

I wasn't saying that casein is not slowly digested. I know that it is.
The part I would have liked references on was when you said that casein is the ONLY slowly digesting protein source, which I believe to be incorrect.

The studies you cited do not compare casein to other proteins so there is nothing to back the above assumption.

Casein may very well be slower to release than egg protein, but the difference probably isn't anything significant.
So as long as you are not taking whey for your night time protein, your fine.


I have to add that I'm not trying to bad mouth casein. I would be using it myself were it not for it being associated with increased cancer risk, whether that turns out to be true or not.
And since there are alternatives (like egg protein), I prefer not to risk it.

[mike250]

I believe the reason Casein protein is considered a slow-digesting protein is because it forms a “gel” in the gut, which results in a steady release of amino acids into the blood stream over time. Egg protein is readily digested and absorbed.

[chrisp2]

Check these out:

http://cebp.aacrjour...stract/10/5/555
http://www.sare.org/...-html/0499.html
http://cebp.aacrjour...bstract/9/1/113

None of them say great things about casein - with respect to cancer. (Not saying I'm going casein free - but I am concerned about adding more to my diet than is already there)

[ajnast4r]

Casein may very well be slower to release than egg protein, but the difference probably isn't anything significant.

asuming the stomach is empty and nothing else is consumed with it...

egg releases for about 4 hours
casein for about 7

both are significantly increased especially when consumed w/ fiber and/or fat.



egg is ideal ...

[neogenic]

I wasn't saying that casein is not slowly digested. I know that it is.
The part I would have liked references on was when you said that casein is the ONLY slowly digesting protein source, which I believe to be incorrect.

The studies you cited do not compare casein to other proteins so there is nothing to back the above assumption.

Casein may very well be slower to release than egg protein, but the difference probably isn't anything significant.
So as long as you are not taking whey for your night time protein, your fine.


I have to add that I'm not trying to bad mouth casein. I would be using it myself were it not for it being associated with increased cancer risk, whether that turns out to be true or not.
And since there are alternatives (like egg protein), I prefer not to risk it.

I've read many studies comparing casein to soy, casein to whey...I am not sure about egg vs. casein.

Casein is favorable to soy in most studies I've read and whey has greater anabolism and nitrogen retention. Its obvious whey would be better over casein for that given its level of assimilation and BV. WPI would be higher and WPH higher still. Dr. Jose Antonio, President of CISSN did a review on casein and whey recently and concluded 80% whey and 20% casein would be ideal post workout and the reverse ratio (80% casein and 20% whey at night). There are probably 20-30 studies I've seen comaring casein to other proteins in a number of parameters/values. Like I said I can't think of one with egg. I can post them here...it would be alot...if wanted.

Correlation to cancer. Uggh. I have my masters in nutritional biochemistry from a school of public health and so many things from the nurses' study, etc. were like that...so many confounding variables. I have not seen that study, I'll have to search. There is no plausibility to such a relationship. Micellar casein or a WPI is amino acids. Soy protein isolate or something along those lines have the isoflavone content that has endocrinological impact that affects an entire cascade and rhythm. That I can see being wary of...micellar casein, Whey Protein Isolate, Hydrolyzed Casein or Whey, egg white or albumin...not so much. The more isolated the protein is (like the powders) the more its about amino acid profiles over anything else. Heck the sweetener or the food coloring in the powder is more debatable in my mind.

[komputerhead]

Hello

Casein is made from cows milk which is usually the A1 protein which is responsible for diabetes and many other problems, see below link.

Most mammals make A2 milk unfortunately due to some genetic variant we mainly have cows that produce the A1 protein which is not ideal for us.

http://www.nzfsa.gov...a1-a2/index.htm

There are companies in New Zealand that produce A2 milk but it has been slow going.

[zoolander]

People seem to be reading different article to me. I've read more than a handful of studies, all good, about whey, casein and soy protein.

[dannov]

Casein is the slowest to release, especially micellar casein.  It seems odd to assume a milk protein that is much like that given to all mammals to maintain life is getting put down over animal flesh or embryos.  Certainly soy is steeped in controversy and the only pro-side is supported by the industry.  Affecting the endrinological cascade can have drastic impact, especially on the hypogonadal, pubescent, and infant/toddlers.   Certainly cow's milk can be a negative for infants due to osmolarity and mineral content differences and their undeveloped gut...leading to diarrhea.

Whey and casein have so many positive studies.  There is genius (in God) to make a fast and slow protein combined.  Rapid acting and long acting.  As far as anti catabolic/anabolic/nitrogen retention its unsurpassed.

A New study showing the benefit of Whey/Casein/Calcium:
: Br J Nutr. 2007 Aug 13;:1-8 [Epub ahead of print] Links
High-calcium diet with whey protein attenuates body-weight gain in high-fat-fed C57Bl/6J mice.Pilvi TK, Korpela R, Huttunen M, Vapaatalo H, Mervaala EM.
Foundation for Nutrition Research, PO Box 30, FIN-00390 Helsinki, Finland.

An inverse relationship between Ca intake and BMI has been found in several studies. It has been suggested that Ca affects adipocyte metabolism via suppressing 1,25-dihydroxycholecalciferol (1,25(OH)2-D3) and decreases fat absorption. We studied the effect of Ca and milk proteins (whey and casein) on body weight in C57Bl/6J mice. Male mice, age 9 weeks, were divided into three groups (ten mice per group) receiving modified high-fat (60 % of energy) diets. Two groups received a high-Ca diet (1.8 % calcium carbonate (CaCO3)), with casein or whey protein (18 % of energy), and one group received a low-Ca diet (0.4 % CaCO3) with casein for 21 weeks. Food intake was measured daily and body weight twice per week. Body fat content (by dual-energy X-ray absorptiometry) of all mice and faecal Ca and fat excretion of seven mice/group were measured twice during the study. Final body weight (44.1 (sem 1.1) g) and body fat content (41.6 (sem 0.6) %) were significantly lower (P < 0.05) in the high-Ca whey group than in the low-Ca casein group (48.1 (sem 0.8) g and 44.9 (sem 0.8) %). Body weight and body fat content of the high-Ca casein group did not differ significantly from the low-Ca casein group even though serum 1,25(OH)2-D3 levels were significantly lower (P < 0.001) in both high-Ca groups than in the low-Ca casein group. Thus changes in serum 1,25(OH)2-D3 do not seem to affect body weight in this animal model. There was a significant difference in fat excretion between the high-Ca whey and low-Ca casein groups (3.9 (sem 0.9) % in the high-Ca whey v. 1.4 (sem 0.2) % in the low-Ca casein group; P < 0.05), which may partly explain the effect on body weight.

How about a full breakdown all all of milk's components from a reivew:
J Exp Ther Oncol. 2007;6(2):89-106.Links
Milk-derived proteins and peptides of potential therapeutic and nutritive value.Zimecki M, Kruzel ML.
Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wroclaw, Poland.

Milk and colostrum are rich in proteins and peptides which play a crucial role in development of the immune system in mammalian offspring. Immunotropic properties of these compounds prompted investigators to search for their utility in prevention and therapy of various disorders in humans. The following constituents of milk are of particular interest: 1) Lactoferrin (LF)--exhibits antibacterial, antifungal, antiviral, antiparasite and antitumor activities. It is protective with regard to intestinal epithelium, promotes bone growth and accelerates recovery of the immune system function in immunocompromised animal; 2) A Proline-Rich Polypeptide (PRP) shows a variety of immunotropic functions, including promotion of T-cell maturation and inhibition'of autoimmune disorders. PRP was recently found to improve or stabilize the Instrumental Activity of Daily Living status in Alzheimer's disease patients. 3) Casein--has been protective in experimental bacteremia by eliciting myelopoiesis. Casein hydrolyzates were also protective in diabetic animals, reduced the tumor growth and diminished colicky symptoms in infants. Casein-derived peptides have been found to have antihypertensive effects. Glycomacropeptide (GMP)--a peptide derived from kappa casein, exhibits antibacterial and antithrombotic activities. 4) Alpha lactalbumin (LA)--demonstrates antiviral, antitumor and anti-stress properties. LA-enriched diets were anxiolytic, lowered blood pressure in rats, prevented diarrhea and led to a better weight gain in malnourished children. 5) Lysozyme--is effective in treatment of periodentitis and prevention of tooth decay. Milk enriched in lysozyme was used in feeding premature infants suffering from concomitant diseases. 6) Lactoperoxidase--shows antibacterial properties. In conclusion, milk-derived proteins and peptides are bio-accessible and safe for the prevention and treatment of numerous disorders in humans.

Aye, however, that cow milk is meant for cows. It is nothing like milk generated for humans. A big problem is that cows are being stimulated with Bovine Hormone Serum to produce a lot more milk than they ought to, resulting in them getting frequent and massive infections which are then treated with antibiotics. These antis stay in their systems for days or weeks, and one of the ways in which they are expelled is--you guessed it, out into the milk you drink. The standards for regulating aren't nearly as strict as you might think.

http://www.notmilk.com

^^ Read the others Zoolander.

[krillin]

Has anyone read this paper? The abstract just screams out for you to read the whole thing to see how they skewer the A2 promoters. (I do disagree with the statement that there is no adverse effect of A1 milk. If you have the wrong HLA genotype, then milk can increase your risk of type I diabetes, and I wouldn't count on A2 being safe.)

Eur J Clin Nutr. 2005 May;59(5):623-31.
Comment in:
Eur J Clin Nutr. 2006 Jul;60(7):921-4; reply 924-5.
Eur J Clin Nutr. 2006 Mar;60(3):437-9.
The A2 milk case: a critical review.
Truswell AS.
Human Nutrition Unit, University of Sydney, Australia. s.truswell@mmb.usyd.edu.au

This review outlines a hypothesis that A1 one of the common variants of beta-casein, a major protein in cows milk could facilitate the immunological processes that lead to type I diabetes (DM-I). It was subsequently suggested that A1 beta-casein may also be a risk factor for coronary heart disease (CHD), based on between-country correlations of CHD mortality with estimated national consumption of A1 beta-casein in a selected number of developed countries. A company, A2 Corporation was set up in New Zealand in the late 1990s to test cows and market milk in several countries with only the A2 variant of beta-casein, which appeared not to have the disadvantages of A1 beta-casein.The second part of this review is a critique of the A1/A2 hypothesis. For both DM-I and CHD, the between-country correlation method is shown to be unreliable and negated by recalculation with more countries and by prospective studies in individuals. The animal experiments with diabetes-prone rodents that supported the hypothesis about diabetes were not confirmed by larger, better standardised multicentre experiments. The single animal experiment supporting an A1 beta-casein and CHD link was small, short, in an unsuitable animal model and had other design weaknesses.The A1/A2 milk hypothesis was ingenious. If the scientific evidence had worked out it would have required huge adjustments in the world's dairy industries. This review concludes, however, that there is no convincing or even probable evidence that the A1 beta-casein of cow milk has any adverse effect in humans.This review has been independent of examination of evidence related to A1 and A2 milk by the Australian and New Zealand food standard and food safety authorities, which have not published the evidence they have examined and the analysis of it. They stated in 2003 that no relationship has been established between A1 or A2 milk and diabetes, CHD or other diseases.

PMID: 15867940

[zoolander]

dannov, correct me if I am wrong but the link that you provided (notmilk.com) looks at negative studies related to consuming whole milk. I'm referring to studies that used isolated proteins from whole milk and soy beans.

Here let's play a game. You provide a refernce for a negative study for an protein isolate from milk and I'll provide 10 positive studies about isolated proteins strengthening the immune system, building muscle and preventing sarcopenia, anti-carcinogenics and so on.

[dannov]

Aye, I get the two confused some.