Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-CoA synthetases of porcine heart and Escherichia coli
- 23 September 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (19) , 5420-5425
- https://doi.org/10.1021/bi00367a012
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 4 references indexed in Scilit:
- REACTION OF SUBSTRATES WITH S-35 THIOPHOSPHORYLATED SUCCINYL-COA SYNTHETASE OF PIG-HEART - SIMILARITIES TO THE CASE OF THE ESCHERICHIA-COLI ENZYME1985
- Capacity for alternating sites cooperativity in catalysis by succinyl-coenzyme A synthetase.Proceedings of the National Academy of Sciences, 1981
- Subunits of succinyl-coenzyme A synthetase: coordination of production in Escherichia coli and discovery of a factor that precludes refoldingJournal of Bacteriology, 1980
- SUCCINIC THIOKINASE .4. IMPROVED METHOD OF PURFICATION ARSENOLYSIS OF GUANOSINE TRIPHOSPHATE SUCCINATE-DEPENDENT GUANOSINE TRIPHOSPHATASE ACTIVITY AND SOME OTHER PROPERTIES OF ENZYME1967