Jun 1, 1976

Arylamidases in normal and diseased human muscle

Clinica Chimica Acta; International Journal of Clinical Chemistry
N C Kar, C M Pearson

Abstract

Human skeletal muscle homogenates were found to contain enzymes that catalyze the hydrolysis of beta-naphthylamides of leucine, arginine and lysine, known substrates for neutral and basic arylamidases. They also contained a trace of activity towards alpha-aspartyl-beta-naphthylamide. The muscle arylamidases were found to be inhibited by p-chloromercuribenzoate, Hg2+ and puromycin. Leucyl, arginyl and lysysl arylamidases were slightly activated by cobalt ions. When compared to controls, no significant differences in muscle arylamidase activities were observed in patients with muscular dystrophies and certain denervating diseases.

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Citations

Mentioned in this Paper

Mercury
Enzymes, antithrombotic
Methoxyleucine Aminopeptidase
Myopathy
Puromycin Dihydrochloride
Aminopeptidase
Lysine
Puromycin Hydrochloride
Enzymes for Treatment of Wounds and Ulcers
Arginine

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