By M L Anson; Kenneth Bailey; John T Edsall
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Additional resources for Advances in protein chemistry. / Volume 9
Available evidence concerning the biosynthesis of serine and glycine, though at present indirect and sometimes even 44 H . R . V. ARNSTEIN contradictory, suggests that carbohydrate is the ultimate source of most, of the aerine and glycine, other than that arising from threonine. The observation (Swick, Buchanan, and Nakao, 1953) that identical amounts of C14 were fixed into the carboxyl groups of glycine, serine, and alanine when rats, whose diets contained similar amounts of these amino acids, were exposed for long periods to radioactive carbon dioxide suggests strongly that these amino acids have a common precursor which is able to fix carbon dioxide.
Like serine, only the L- form of threonine gives rise to glycine, but METABOLISM OF GLYCINE 39 the liver enzymes which cleave serine and threonine are not identical (Vilenkina, 1952). The cleavage of threonine into glycine also differs from that of serine since it is irreversible (Elliott and Neuberger, 1950). In the intact animal, glycine formation from threonine occurs only to a limited extent. Thus, threonine is utilized by the rat only about onetenth as efficiently as glycine or serine for hippuric acid synthesis (Meltzer and Sprinson, 1952; Chao, Delwiche, and Greenberg, 1953).
3 g. 5 g. of this amino acid. 2 g. glycine. 2 g. per day and the amount of body protein synthesized daily was therefore approximately 200 mg. per rat. 8 g. 1 g. 9 g. or about 48 mg. 8 millimole per day per 100 g. body weight). 34 H . R. V . 6 mg. glycine per day per 100 g. body weight). In these calculations no allowance has been made for the amount of serine in the diet. 9 % (Rees, 1946) and rat body protein about 5 % (Sauberlich and Baumann, 1951) of serine. The djfference between the amount of serine eaten and that required for protein synthesis may be calculated to be approximately 75 mg.
Advances in protein chemistry. / Volume 9 by M L Anson; Kenneth Bailey; John T Edsall