Complexes of chicken heart lactic dehydrogenase with coenzymes and substrates
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference7 articles.
1. Reduction of Aldehydes, Ketones and Acid Chlorides by Sodium Borohydride
2. Evidence for ternary-complex formation with rabbit-muscle lactic acid dehydrogenase, diphosphopyridine nucleotide and pyruvic acid
3. Determination of Dissociation Constants of Coenzymes and Abortive Ternary Complexes with Rabbit Muscle Lactate Dehydrogenase from Fluorescence Measurements
4. The kinetics of the reversible inhibition of heart lactate dehydrogenase through the formation of the enzyme–oxidized nicotinamide–adenine dinucleotide–pyruvate compound
5. LACTIC DEHYDROGENASE
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1. Impact of High Pyruvate Concentration on Kinetics of Rabbit Muscle Lactate Dehydrogenase;Applied Biochemistry and Biotechnology;2011-05-31
2. Cardioprotective activity of a novel and potent competitive inhibitor of lactate dehydrogenase;FEBS Letters;2009-11-12
3. Activity of heart and muscle lactate dehydrogenases in all-aqueous systems and in organic solvents with low amounts of water. Effect of guanidine chloride;European Journal of Biochemistry;1992-04
4. THR246 mutations decrease substrate inhibition in lactate dehydrogenase;Biochemical and Biophysical Research Communications;1992-02
5. Spectroscopic and kinetic characterization of nonenzymic and aldose reductase mediated covalent NADP-glycolaldehyde adduct formation;Biochemistry;1990-10-01
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