Zur Spezifität der Arginase.

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Abstract
It was necessary for the substrate to have free guanidine and carboxyl groups. Every change in these interfered with arginase action. Enzyme preps. were obtained from livers of hog, ram, cattle, rabbit, and dog. An acid radical, peptide group, or methyl or hydroxyl groups could be substituted in the [alpha] amino group of the substrate. The length of the carbon chain varied. For all the derivatives of arginine tested, the optimum pH for arginase action was 7, with a range, of 7-8. Karashima''s finding that liver extract hydrolyzed guanidine-acetic acid was confirmed. Arginine and guanidine-acetic acid were probably hydrolyzed by different enzymes.

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