Room temperature phosphorescence of Trp-314 as a monitor of subunit communications in alcohol dehydrogenase from horse liver
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00453a028
Reference34 articles.
1. Properties of bound trifluoroethanol complexes with horse liver alcohol dehydrogenase
2. Biphasic transient kinetics are a property of a single site in horse liver alcohol dehydrogenase
3. Fluorinated ligands as NMR probes of active-site nonequivalence in abortive ternary complexes of horse liver alcohol dehydrogenase
4. The Use of Biochemical Solid-Phase Techniques in the Study of Alcohol Dehydrogenase. 2. Selective Carboxymethylation of Bioaffinity-Bound Alcohol Dehydrogenase
5. Kinetic Equivalence of the Subunits of Liver Alcohol Dehydrogenase
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