The specificity of arginase: action upon argininic acid

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Abstract
Argininic acid was split by liver extracts into urea and l([long dash])-a-hydroxy-8-amino-n-valeric acid. The latter product was isolated and identified. Under favorable conditions 90% of the substrate was hydrolysed. The enzyme responsible was identical with arginase, because it had the same pH optimum and in the presence of Co its action was magnified in exactly the same degree. Susceptibility to arginase was therefore not absolutely dependent upon the presence of an intact or a modified a-amino group. This group exerted, nevertheless an extremely important influence; for argininic acid was hydrolysed by arginase about 3750 times less actively than arginine.

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