AND ALEXANDER RUTENBURG, M. M.D. demonstration of "leucylpeptidase" as a component of erepsin was made by measuring the rate of liberation o carboxyl f groups from L-leucylglycine.6 However, since this substrate was hydrolyzed by enzymes other than leucylpeptidase, L-leucinamide, a more specific substrate was synthesized.' Gomori4 developed a more precise colorimetric and histe chemical method to study tissue aminopeptidase, based on the formation of azo dyes from the naphthylamine moiety liberated by enr zymatic hydrolysis of glycyl- o alanyl-p-naphthylamide. Green et a1.6 and Folk and Burstones assayed enzymatic activity of mammalian tissues and serum by measuring the p-naphthylamine liberated by hydrolysis of L-leucylP-naphthylamide hydrochloride. T h e present report deals with a new method for the colorimetric measurement o leucine f aminopeptidase activity in urine and an improved procedure for the assay of enzymatic activity in tissues and serum, the kinetics o f the urinary and serum enzyme, and the assay of this enzyme in the urine and serum of normal subjects and patients with cancer and other diseases. HE FIRST 0.00 137M solution of L-leucyl-8-naphthylamide METHODS Reagents. T h e reagents used included the following: a substrate solution composed of a From the departments of Surgery, Beth
Cancer – Wiley
Published: Mar 1, 1958
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