Home
Resources
Publications
Interaction of Trypsin-Like Protease From Streptomyces Griseus With an Immobilized Inhibitor From Kidney Bean

Interaction of Trypsin-Like Protease From Streptomyces Griseus With an Immobilized Inhibitor From Kidney Bean

V V Mosolov, N V Fedurkina, T A Valueva

Biochim Biophys Acta. 1978 Jan 12;522(1):187-94.

PMID: 413581

Abstract:

An immobilized double-headed inhibitor from Phaseolus vulgaris L. selectively binds the trypsin-like enzyme produced by Streptomyces griseus. Binding takes place at pH 8.0, and at pH 2.0 the protease can be quantitatively released from the complex. Purified by affinity chromatography, the trypsin-like enzyme is homogeneous according to polyacrylamide gel electrophoresis and ultracentrifugation data. Physico-chemical and enzymic properties of the enzyme are identical to those exhibited by the enzyme purified by ion-exchange chromatography. Chymoelastases from Str. griseus as well as the subtilisin-like enzyme do not interact with an immobilized inhibitor. In solution, the inhibitor from P. vulgaris gives a stable ternary complex with bovine trypsin and chymotrypsin, whereas with an immobilized inhibitor the trypsin, if present, tends to displace chymotrypsin in an chymotrypsin inhibitor complex. This evidence suggests that immobilization results in considerable changes in inhibitor properties.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9036060	Protease from Streptomyces griseus		9036-06-0	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: