A study of the quenching of the intrinsic fluorescence of succinyl-CoA synthetase from Escherichia coli by acrylamide, iodide, and coenzyme A
- 1 August 1983
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 22 (18) , 4272-4275
- https://doi.org/10.1021/bi00287a017
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 3 references indexed in Scilit:
- Fluorescence detection of increased local flexibility induced by coenzyme A in succinyl-CoA synthetase from Escherichia coliBiochemistry, 1982
- AFFINITY LABELING OF SUCCINYL-COA SYNTHETASE FROM PORCINE HEART AND ESCHERICHIA-COLI WITH OXIDIZED COENZYME-A DISULFIDE1978
- Fluorescent Probes for Conformational States of Proteins. II. The Binding of 2-p-Toluidinylnaphthalene-6-sulfonate to α-Chymotrypsin*Biochemistry, 1967