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Egg protein

Egg protein has always been the gold standard by which all other proteins are measured. Egg protein has a PDCAAS (Protein Digestibility Corrected Amino Acid Score) score of number 1 the highest value possible, it has a Bv (biological value) of 100 and a highly balanced amino acid profile. Meaning your body can not find a protein source with a better conversion rate to muscle! This is critical component in achieving phenomenal muscle growth, not surprising as eggs contain many naturally occurring highly anabolic substrates. When the protein levels and substrates are enhanced to optimise absorption you get a highly anabolic protein.

Egg protein has been a highly prized protein source for millennia from the humble hunter gathers who searched for this prized food through to the many mighty warrior tribes who have all held the egg high as a prized source of power for the human body. Egg protein has only reduced in popularity over the past few decades due to some bad press with regard to the fat content which would appear to be slightly misleading and rise purified milk proteins left over from cheese production.

As recently as the golden era of bodybuilding eggs have been highly valued by such notables a Vince Gironda, Rheo Blair and even old numero uno, Arnie (Quote: milk is for babies!). In fact back in the 70’s Vince Gironda was promoting the value of fertile eggs.

This is an interesting fact as recent research indicates that their are a few highly anabolic elements potentially present in egg protein Arachidonic Acid being one and the presence of follistatin being the other.

As the major percentage of fat in egg yolk is made of good fat when the eggs are from a good source it is very interesting to review recent research into the positive hormonal effects of these essential fatty acids Read more: Arachidonic Acid.

Whilst we are no way claiming to have extracted or increased the next substrate Follistin it is not surprising to find that the naturally occurring with in egg yolk. What is Follistatin? Read more: Follistatin, follistatin has been identified as a natural Myostatin Antagonist (blocker).

Mysotatin is TGF beta protein that inhibits muscle growth! http://en.wikipedia.org/wiki/Myostatin.

Our specific processing of our egg products, as egg protein specialists means you can rest assured that that all products do not experience any thermal degradation which may damage any amino acids, enzymes or substrates. We produce AEM with added co-factors to enhance absorption and optimise the anabolic nature of the product, naturally. Our eggs are from high end flocks and our solids gently filtered and dessicated via cool mist chambers creating what we call a fertile isolate powder. The easily dispersible powder is blended with additional co-factors and flavoured to creating a easily mixable great tasting superior protein source.

See Nutrient Absorption for information on additional added co-factors for increased absorption and Growth Factors for data on added elements for enhanced anabolic activity.

 

References:

Andersson, A., A. Sjodin, A. Hedman, R. Olsson, and B. Vessby. Fatty acid profile of skeletal muscle phospholipids in trained and untrained young men. Am J Physiol Endocrinol Metab. 279:E744-751, 2000.

Aronson, D., M. D. Boppart, S. D. Dufresne, R. A. Fielding, and L. J. Goodyear. Exercise stimulates c-Jun NH2 kinase activity and c-Jun transcriptional activity in human skeletal muscle. Biochem Biophys Res Commun. 251:106-110, 1998.

Boppart, M. D., D. Aronson, L. Gibson, R. Roubenoff, L. W. Abad, J. Bean, L. J. Goodyear, and R. A. Fielding. Eccentric exercise markedly increases c-Jun NH(2)-terminal kinase activity in human skeletal muscle. J Appl Physiol. 87:1668-1673, 1999.

Boppart, M. D., S. Asp, J. F. Wojtaszewski, R. A. Fielding, T. Mohr, and L. J. Goodyear. Marathon running transiently increases c-Jun NH2-terminal kinase and p38 activities in human skeletal muscle. J Physiol. 526 Pt 3:663-669, 2000.

Glass, D. J. Molecular mechanisms modulating muscle mass. Trends Mol Med. 9:344-350, 2003.

Griendling, K. K., D. Sorescu, B. Lassegue, and M. Ushio-Fukai. Modulation of protein kinase activity and gene expression by reactive oxygen species and their role in vascular physiology and pathophysiology. Arterioscler Thromb Vasc Biol. 20:2175-2183, 2000.

Levonen, A. L., R. P. Patel, P. Brookes, Y. M. Go, H. Jo, S. Parthasarathy, P. G. Anderson, and V. M. Darley-Usmar. Mechanisms of cell signaling by nitric oxide and peroxynitrite: from mitochondria to MAP kinases. Antioxid Redox Signal. 3:215-229, 2001.

Lu, J., T. A. McKinsey, R. L. Nicol, and E. N. Olson. Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases. Proc Natl Acad Sci U S A. 97:4070-4075, 2000.

Rao, G. N., N. R. Madamanchi, M. Lele, L. Gadiparthi, A. C. Gingras, T. E. Eling, and N. Sonenberg. A potential role for extracellular signal-regulated kinases in prostaglandin F2alpha-induced protein synthesis in smooth muscle cells. J Biol Chem. 274:12925-12932, 1999.

Trappe, T. A., F. White, C. P. Lambert, D. Cesar, M. Hellerstein, and W. J. Evans. Effect of ibuprofen and acetaminophen on postexercise muscle protein synthesis. Am J Physiol Endocrinol Metab. 282:E551-556, 2002.

Wilborn, C, M Roberts, C Kerksick, M Iosia, L Taylor, B Campbell, T Harvey, R Wilson, M. Greenwood, D Willoughby and R Kreider. Exercise & Sport Nutrition Laboratory, Center for Exercise, Nutrition & Preventive Health Research, Baylor University, Waco, TX 76798-7313.

http://en.wikipedia.org/wiki/Arachidonic_acid

http://en.wikipedia.org/wiki/Prostaglandins

http://www.nutros.com/nsr-0502t.html#_101