Interaction of coenzyme with differently prepared zinc-free (apo) horse liver alcohol dehydrogenases.
Abstract: No abstract available
Publication Date: 1969-11-10 PubMed ID: 4310828
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- Comparative Study
- Journal Article
Cite This Article
APA
Hoagstrom CW, Iweibo I, Weiner H.
(1969).
Interaction of coenzyme with differently prepared zinc-free (apo) horse liver alcohol dehydrogenases.
J Biol Chem, 244(21), 5967-5971.
Publication
Researcher Affiliations
MeSH Terms
- Acetates
- Alcohol Oxidoreductases / analysis
- Animals
- Antibodies
- Antigens
- Binding Sites
- Chemical Phenomena
- Chemistry
- Dialysis
- Edetic Acid
- Fluorescence
- Fluorometry
- Horses
- Hydrogen-Ion Concentration
- Immunodiffusion
- Kinetics
- Liver / enzymology
- NAD
- Rabbits
- Succinates
- Sulfhydryl Compounds / analysis
- Zinc
Citations
This article has been cited 2 times.- Tiwari MK, Singh RK, Singh R, Jeya M, Zhao H, Lee JK. Role of conserved glycine in zinc-dependent medium chain dehydrogenase/reductase superfamily.. J Biol Chem 2012 Jun 1;287(23):19429-39.
- Schneider G, Eklund H, Cedergren-Zeppezauer E, Zeppezauer M. Structure of the complex of active site metal-depleted horse liver alcohol dehydrogenase and NADH.. EMBO J 1983;2(5):685-9.
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