I'm far too hard to worry about that!Originally Posted by goose4
English Rudeboy
I'm far too hard to worry about that!
Banned
I know your one hard bloke,I wish I was as hard as youI'm far too hard to worry about that!
English Rudeboy
Cialis is the key homeslice!I know your one hard bloke,I wish I was as hard as you
Banned
I thought it was Charlie,LOL.Good luck on your cycle its time to get massive mate!!!Cialis is the key homeslice!
English Rudeboy
Oh it's well under way baby - this one is "Operation Get Shredded" and it is progressing nicely...
Banned
Ok this is for you my sister sent it to me,we were talking about this.
http://www.feinberg.northwestern.edu...ts/biotin.html
Quote:
Physiologic Functions
Biotin coenzyme participates in carboxylation reactions as a carrier of carbon dioxide and donor of carboxyl groups to substrates. The carboxylation step is rate-limiting in fatty acid synthesis. Carboxylation steps are also required in conversion of pyruvate to oxaloacetate which drives the Kreb's cycle, in metabolism of odd chain fatty acids by converting propionyl CoA to methylmalonyl CoA, and in catabolism of leucine.
Factor Affecting Availability
Chronic consumption of raw egg whites reduces biotin availability by binding with avidin to form a nonabsorbable complex.
Deficiency
Biotin deficiency is rarely observed since it is widely available in foods. Inherited defects in biotin metabolism develop biotin deficiency as might patients receiving incomplete parenteral nutrition and infants consuming human milk with low biotin content due to poor maternal intake. Signs of biotin deficiency include hair loss, dermatosis, anorexia, nausea, weight loss, muscle pains, and localized loss of sensation.
The Journal of Nutrition Vol. 128 No. 10 October 1998, pp. 1716-1722
Egg proteins contribute substantially to the daily nitrogen allowances in Western countries and are generally considered to be highly digestible. However, information is lacking on the true ileal digestibility of either raw or cooked egg protein. The recent availability of stable isotope-labeled egg protein allowed determination of the true ileal digestibility of egg protein by means of noninvasive tracer techniques. Five ileostomy patients were studied, once after ingestion of a test meal consisting of 25 g of cooked 13C- and 15N-labeled egg protein, and once after ingestion of the same test meal in raw form. Ileal effluents and breath samples were collected at regular intervals after consumption of the test meal and analyzed for 15N- and 13C-content, respectively. The true ileal digestibility of cooked and raw egg protein amounted to 90.9% (cooked) and 51.3% (raw) respectively. A significant negative correlation (r = 0.92, P < 0.001) was found between the 13C-recovery in breath and the recovery of exogenous N in the ileal effluents. In summary, using the 15N-dilution technique we demonstrated that the assimilation of cooked egg protein is efficient, albeit incomplete, and that the true ileal digestibility of egg protein is significantly enhanced by heat-pretreatment. A simple 13C-breath test technique furthermore proved to be a suitable alternative for the evaluation of the true ileal digestibility of egg protein........
Egg white protein is generally considered to be less digestible than heat-pretreated egg white protein. In this study, it was shown that after ingestion of 25 g of raw egg protein, almost 50% is malabsorbed over 24 h. The higher digestibility of cooked egg protein presumably results from structural changes in the protein molecule induced by heating, thereby enabling the digestive enzymes to gain broader access to the peptide bonds. It has been suggested that the reduced digestibility of raw egg white is at least partially related to the presence of trypsin inhibitors in raw egg white.
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