A comparative study of arginase and canavanase

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Abstract
The 2 enzymes showed only-such differences (optimum pH, optimum substrate conc. and Michaelis constant) in their kinetics as were to be expected from the nature of the substrates. Otherwise, there was a close parallelism between arginase and canavanase actions. In tissues and blood of different animals they were either present together or not at all and in every case the action on canavanine was slower than that on arginine. By no procedure was it possible to reverse this quantitative relationship and obtain a prep. in which canavanase activity was stronger than arginase activity. In any particular prep., factors affecting arginase influenced canavanase in the same direction and often to the same extent, e.g., the loss of activity on autolysis and the increase in activity in the presence of cobalt ions affected both enzymes equally. In the presence of Co the pH-optima for the 2 reactions became identical at pH 7.5. The balance of evidence was thus in favor of the 2 enzymes being identical.