Abstract
Summary
Arginine-glycine transamidinase, one of the 2 enzymes concerned with the biosynthesis of creatine from amino acid precursors, has been found to occur in high concentration in mammalian pancreas. Homogenates of dog pancreas have approximately 5 times the transamidinase activity of kidney homogenates from the same animal, on a wet weight basis. The assay systems by which these tissues were compared included (a) canavanine-ornithine transamidination, made unidirectional by the addition of a carbonyl compound to trap canaline, and (b) arginine-hydroxylamine transamidination. It is suggested that the ability to catalyze these latter two reactions is a characteristic property of transamidinases. Chemical and enzymic syntheses of hydroxyguanidine are described.
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