Abstract
Numerous biochemical properties (e.g. Mr, carbohydrate content, pI) were determined for kallikrein isolated from rat submandibular glands by a simple, rapid purification procedure. The kinetic behaviour of the enzyme towards various inhibitors and synthetic substrates was investigated. The effects of different salts and detergents on the esterolytic activity of the rat tissue kallikrein were recorded.
MeSH terms
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Animals
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Arginine / analogs & derivatives
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Detergents / pharmacology
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Hydrogen-Ion Concentration
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In Vitro Techniques
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Kallikreins / antagonists & inhibitors
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Kallikreins / isolation & purification*
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Kallikreins / metabolism
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Kinetics
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Male
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Oligopeptides
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Rats
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Salts / pharmacology
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Submandibular Gland / enzymology*
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Substrate Specificity
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Temperature
Substances
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Detergents
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Oligopeptides
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Salts
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Val-Leu-Arg-p-nitroanilide
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Arginine
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Kallikreins