Circular dichroism of complexes of NADH with self-associating bovine liver glutamate dehydrogenase
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
Reference26 articles.
1. Molecular weight of the subunits, oligomeric and associated forms of bovine liver glutamate dehydrogenase
2. Glutamate Dehydrogenase: Amino-Acid Sequence of the Bovine Enzyme and Comparison with That from Chicken Liver
3. Bovine Liver Glutamate Dehydrogenase
4. Binding by Glutamate Dehydrogenase of Reduced Diphosphopyridine Nucleotide
5. The binding of NADH by glutamate dehydrogenase as measured by polarization of fluorescence
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1. Studying NAD(P)H cofactor-binding to alcohol dehydrogenases through global analysis of circular dichroism spectra;Physical Chemistry Chemical Physics;2019
2. Branched-chain Amino Acid Metabolon;Journal of Biological Chemistry;2010-01
3. The Binding of Oxidised Coenzyme to Bovine-Liver Glutamate Dehydrogenase Studied by Circular-Difference Spectroscopy;European Journal of Biochemistry;2005-03-03
4. Fluorescence stopped-flow studies on the binding of 1,N6-etheno-NAD to bovine liver glutamate dehydrogenase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1988-08
5. The Binding of NADH and NADPH to Bovine-Liver Glutamate Dehydrogenase. Spectroscopic Characterisation;European Journal of Biochemistry;1982-10
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