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PMID: 6188466 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Localization of the proteinase-induced thiol groups in alpha 2-macroglobulin.

Biochemical and biophysical research communications ·Vol. 111 ·No. 3 ·1983-03-29 ·Pages 964-9

Pochon F, Favaudon V, Bieth J

Abstract

Free thiol groups released on proteolytic attack of alpha 2-macroglobulin by trypsin or chymotrypsin bind covalently to thiopropyl-Sepharose, indicating that they are located at the surface of the complexes. These cysteine sulfhydryl groups appear to be in contact with the alpha 2M-bound proteases from singlet-singlet energy transfer measurements between fluorescein isothiocyanate-labeled proteinases and N-(iodoacetylaminoethyl)-5-naphtylamine-1-sulfonic acid-labeled thiols in alpha 2-macroglobulin.

MeSH Terms
Binding Sites Chromatography, Affinity Chymotrypsin/metabolism Endopeptidases/metabolism Energy Transfer Humans Protein Binding Sulfhydryl Compounds/metabolism Surface Properties Trypsin/metabolism alpha-Macroglobulins/metabolism
Chemicals
Sulfhydryl Compounds alpha-Macroglobulins Endopeptidases Chymotrypsin Trypsin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Pochon F
Favaudon V
Bieth J
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1983-03-29
Pages
964-9
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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