Abstract
In normal and pathological human sera, two distinct l-leucine amide-splitting enzymes were studied. One of them has an optimal activity at pH 9 (“alcaline leucinamidase”) and is activated by Mg 2+ ions. The second has an optimal activity at pH 7.8 (“neutral leucinamidase”) and is inhibited by Mg 2+ ions. A semi-automated method permitting the selective determination of the “alcaline leucinamidase” without interference of the “neutral leucinamidase” is presented here. The authors studied the kinetics of the enzymatic reaction, and the normal and pathological variations, in comparison with other classical enzymes. They concluded that “alcaline leucinamidase” has some of the principal properties of a true leucinaminopeptidase (E.C. 3.4.1.1). Its elevation in human pathological sera is in correlation with transaminases GOT and GPT, but not with alcaline phosphatase nor with leucyl-arylamidase (leucyl-paranitroanilide-splitting enzyme: E.C. 3.4.1.2 or pseudo-LAP). “Alcaline leucinamidase” seems to be an hepatic cytolytic enzyme of much higher sensibility than transaminases.
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