[Interactions between human blood serum inhibitors and native and modified dextran proteinases--terrilytin and trypsin]

Autor:	G M, Lindenbaum, I M, Tereshin
Rok vydání:	1978
Předmět:	Drug Combinations Kinetics Macromolecular Substances alpha 1-Antitrypsin Amylases Humans Dextrans Protease Inhibitors Trypsin alpha-Macroglobulins Peptide Hydrolases Protein Binding
Zdroj:	Biokhimiia (Moscow, Russia). 43(12)
ISSN:	0320-9725
Popis:	Interactions between native terrylytin and trypsin and their derivatives modified by water-soluble dextrans on one hand and human blood serum inhibitors on the other, were studied. It was shown that modification of the enzymes results in changes in the type of their inhibition by blood serum due to a decrease of affinity of polymeric enzyme forms for alpha 2-macroglobulin and alpha 1-antitrypsin. The inhibition constants for native and modified forms of terrylytin and trypsin were calculated. The effects of steric and electrostatic factors on the interaction between inhibitors of blood and polymeric forms of proteinases are discussed.
Databáze:	OpenAIRE
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