Abstract
The metabolic pathways of the deaminated residues of glycine and of alanine have been studied by feeding the amino acids to fasting animals. Alanine readily increased the store of glycogen in the livers of fasting rats whereas glycine did not. When fed to fasting dogs, alanine caused a smaller rise in the catabolism of protein than glycine, as judged by the excretion of inorganic S, presumably because the deaminated residue of alanine but not of glycine forms sugar and so saves protein.

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