Four Isozymic Forms of a Peptidase Resembling Kallikrein. Purified from the Rat Submandibular Gland
- 1 January 1967
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 348 (Jahresband) , 111-118
- https://doi.org/10.1515/bchm2.1967.348.1.111
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.This publication has 6 references indexed in Scilit:
- Purification and characteristics of an alkaline protease from rat-submandibular glandBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966
- Demonstration of a Proteolytic Enzyme, Salivain, in Rat Saliva.Acta Chemica Scandinavica, 1966
- STUDIES IN SALIVARY GLANDS .I. TRYPSIN-LIKE ENZYMES1965
- SNAKE VENOMS, KALLIKREINS, AND KININOGEN*Annals of the New York Academy of Sciences, 1963
- Action of the Kallikreins on Synthetic Ester SubstratesExperimental Biology and Medicine, 1961
- The relationship between glandular activity, bradykinin formation and functional vaso‐dilatation in the submandibular salivary glandThe Journal of Physiology, 1956