Observations on the conformational changes in the structure of a cell surface protease, followed by its ability to be recognised by competitive and non-competitive inhibitors

F S Steven; M M Griffin; M Anees; E W Benbow

doi:10.3109/14756369209020175

Observations on the conformational changes in the structure of a cell surface protease, followed by its ability to be recognised by competitive and non-competitive inhibitors

J Enzyme Inhib. 1992;6(3):251-8. doi: 10.3109/14756369209020175.

Authors

F S Steven¹, M M Griffin, M Anees, E W Benbow

Affiliation

¹ Department of Biochemistry and Molecular Biology, School of Biological Sciences, University of Manchester, UK.

PMID: 1284962
DOI: 10.3109/14756369209020175

Abstract

Lung tumour cells possess a cell surface protease which can be inhibited by a cytoplasmic protein inhibitor extracted from these cells. The dissociation of this enzyme-inhibitor complex on the surface of tumour cells in sections treated with 10(-4) M sodium dodecyl sulphate has been studied. The dissociation of the inhibitor and regain of enzymic activity was followed by the use of a fluorescent probe which binds to the active centre of the cell surface enzyme in a competitive manner.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Aminacrine / metabolism
Binding, Competitive
Carboxylic Ester Hydrolases / antagonists & inhibitors
Carboxylic Ester Hydrolases / metabolism*
Carcinoma / enzymology*
Endopeptidases / metabolism*
Frozen Sections
Humans
Membrane Proteins / metabolism*
Protease Inhibitors / metabolism*
Protein Conformation
Protein Denaturation
Sodium Dodecyl Sulfate
Staining and Labeling

Substances

Membrane Proteins
Protease Inhibitors
Sodium Dodecyl Sulfate
Aminacrine
Carboxylic Ester Hydrolases
guanidinobenzoate esterase
Endopeptidases