Four Isozymic Forms of a Peptidase Resembling Kallikrein. Purified from the Rat Submandibular Gland

Abstract
Four multiple forms (A, B, C and D) of an enzyme capable of hydrolyzing N[alpha]-benzoyl-DL-arginine-p-nitroanilide and [beta]-naphthylamide with very slow rates of hydrolysis of proteins were purified by precipitation and chromatographic methods from the rat submandibular gland. The non-identity of the isoenzymes with each other was ensured in DEAE-cellulose chromatography and starch gel electrophoresis. The molecular weight of A, B and D was found to be about 25, 000 and that of C about 28, 000 when determined by Sephadex gel filtration. Only small quantitative differences could be demonstrated between the preparations in substrate specificity and modifier characteristics studied. An identity of the enzyme with submandibular kallikrein is likely.

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