Binding of coenzyme, coenzyme fragments, and inhibitors to native and carboxymethylated horse liver alcohol dehydrogenase from chlorine-35 nuclear magnetic resonance quadrupole relaxation
- 1 July 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (15) , 3407-3413
- https://doi.org/10.1021/bi00582a030
Abstract
No abstract availableThis publication has 4 references indexed in Scilit:
- Nuclear magnetic resonance studies of chloride binding to proteinsJournal of the American Chemical Society, 1978
- 35Cl nuclear magnetic relaxation studies of Cl− binding to lactate dehydrogenaseArchives of Biochemistry and Biophysics, 1976
- ANOMALOUS ROTATORY DISPERSION OF ENZYME COMPLEXES .V. MECHANISM OF COENZYME BINDING TO LIVER ALCOHOL DEHYDROGENASE1964
- LIVER ALCOHOL DEHYDROGENASE-DPN-PYRAZOLE COMPLEX - A MODEL OF A TERNARY INTERMEDIATE IN ENZYME REACTION1963