Structural arrangement in the alpha 2-macroglobulin--thrombin complex

The cysteine sulfhydryl groups of alpha 2-macroglobulin (alpha 2M) generated upon thrombin complex formation are in contact with the proteinase surface as evidenced by singlet--singlet energy transfer measurements from N-(iodoacetylaminoethyl)-5-naphthylamine-1-sulfonic acid-labeled thiol functions...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 1983-09, Vol.161 (1), p.51-54
Main Authors: Pochon, F, Steinbuch, M, Lambin, P, Kichenin, V
Format: Article
Language:English
Subjects:
alpha-Macroglobulins - metabolism
Chymotrypsin - metabolism
Energy Transfer
Humans
Kinetics
Macromolecular Substances
Thrombin - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The cysteine sulfhydryl groups of alpha 2-macroglobulin (alpha 2M) generated upon thrombin complex formation are in contact with the proteinase surface as evidenced by singlet--singlet energy transfer measurements from N-(iodoacetylaminoethyl)-5-naphthylamine-1-sulfonic acid-labeled thiol functions of alpha 2M to fluorescein isothiocyanate-labeled thrombin. The thrombin-alpha 2M binding is normally covalent, but the presence of hydroxylamine during the reaction leads to the formation of a non-covalent complex. The transfer energy determinations show that the alpha 2M binding sites of thrombin are quite similar, whatever covalent or non-covalent binding occurs.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(83)80728-5