Fluorescence lifetime and anisotropy studies with liver alcohol dehydrogenase and its complexes
- 1 October 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (21) , 6631-6637
- https://doi.org/10.1021/bi00369a045
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 21 references indexed in Scilit:
- Time-resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenaseBiochemistry, 1981
- Transfer of singlet energy within trypsinBiochemistry, 1979
- Site‐Specific Substituted Cobalt(II) Horse Liver Alcohol DehydrogenasesEuropean Journal of Biochemistry, 1979
- The mechanism of quenching of liver alcohol dehydrogenase fluorescence due to ternary complex formation.Journal of Biological Chemistry, 1978
- Fluorescence Quenching and Energy Transfer in Complexes between Horse‐Liver Alcohol Dehydrogenase and CoenzymesEuropean Journal of Biochemistry, 1978
- Exposure of tryptophanyl residues and protein dynamicsBiochemistry, 1977
- Liver alcohol dehydrogenase-coenzyme reaction rates.Journal of Biological Chemistry, 1977
- PH-DEPENDENT CONFORMATIONAL STATES OF HORSE LIVER ALCOHOL-DEHYDROGENASE1977
- LIVER ALCOHOL DEHYDROGENASE-DPN-PYRAZOLE COMPLEX - A MODEL OF A TERNARY INTERMEDIATE IN ENZYME REACTION1963
- Polarization of the fluorescence of macromolecules. 1. Theory and experimental methodBiochemical Journal, 1952