Two sulfhydryl groups near the active site of thiolase I from porcine heart: modification of thiolase with the fluorescent thiol reagent S-mercurio-N-dansyl-L-cysteine
- 1 November 1982
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 21 (24), 6112-6118
- https://doi.org/10.1021/bi00267a013
Abstract
No abstract availableThis publication has 4 references indexed in Scilit:
- Modification of two essential cysteines in rabbit muscle pyruvate kinase by the guanine nucleotide analog 5'-[p-(fluorosulfonyl)benzoyl]guanosineBiochemistry, 1981
- Proton transfer from acetyl-coenzyme A catalyzed by thiolase I from porcine heartBiochemistry, 1981
- Inhibition of fatty acid oxidation by 2-bromooctanoate. Evidence for the enzymatic formation of 2-bromo-3-ketooctanoyl coenzyme A and the inhibition of 3-ketothiolase.Journal of Biological Chemistry, 1979
- A colorimetric method for determining low concentrations of mercaptansArchives of Biochemistry and Biophysics, 1958