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Studies on the interactions of glycerol dehydrogenase from Bacillus stearothermophilus with Zn2+ ions and NADH

Biochimica Et Biophysica Acta

Aug 1, 1990

Paul SpencerMilind Madhukar Gore

PMID: 2378897

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Abstract

The interactions of the essential divalent cation, Zn2+, with the binary complex formed between glycerol dehydrogenase (glycerol:NAD+ 2-oxidoreductase, EC 1.1.1.6) and its coenzyme NADH have been examined by fluorescence spectroscopy. Both the metallo and non-metallo form of the enzyme ...read more

Mentioned in this Paper

Oxidation-Reduction
Fluorescence Spectroscopy
Glycerol dehydrogenase
NADH
Coenzymes
Oxidoreductase
Cations, Divalent
Zinc
Sugar Alcohol Dehydrogenases
Plasma Protein Binding Capacity

Studies on the interactions of glycerol dehydrogenase from Bacillus stearothermophilus with Zn2+ ions and NADH

Biochimica Et Biophysica Acta

Aug 1, 1990

Paul SpencerMilind Madhukar Gore

PMID: 2378897

DOI:

Abstract

The interactions of the essential divalent cation, Zn2+, with the binary complex formed between glycerol dehydrogenase (glycerol:NAD+ 2-oxidoreductase, EC 1.1.1.6) and its coenzyme NADH have been examined by fluorescence spectroscopy. Both the metallo and non-metallo form of the enzyme ...read more

Mentioned in this Paper

Oxidation-Reduction
Fluorescence Spectroscopy
Glycerol dehydrogenase
NADH
Coenzymes

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