The colorimetric determination of leucine aminopeptidase in urine and serum of normal subjects and patients with cancer and other diseases

The colorimetric determination of leucine aminopeptidase in urine and serum of normal subjects... 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 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cancer Wiley

The colorimetric determination of leucine aminopeptidase in urine and serum of normal subjects and patients with cancer and other diseases

Cancer, Volume 11 (2) – Mar 1, 1958

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Publisher
Wiley
Copyright
Copyright © 1958 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0008-543X
eISSN
1097-0142
DOI
10.1002/1097-0142(195803/04)11:2<283::AID-CNCR2820110209>3.0.CO;2-8
Publisher site
See Article on Publisher Site

Abstract

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

Journal

CancerWiley

Published: Mar 1, 1958

References

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