Abstract
1. The binding of NAD+ and NADH to glycerol 3-phosphate dehydrogenase was studied in the pH range 6.0–9.0 at 25°C and in the temperature range 16–43°C at pH7.0. 2. The second-order velocity constants for the combination of NADH with the enzyme in the pH range 6.0–9.0 and for the combination of NAD+ with the enzyme at pH6.0 were determined. 3. The velocity constant for the dissociation of the enzyme–NAD+ complex at pH6.0 was measured.
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- Bentley P., Dickinson F. M. A study of the kinetics and mechanism of rabbit muscle L-glycerol 3-phosphate dehydrogenase. Biochem J. 1974 Oct;143(1):19–27. doi: 10.1042/bj1430019. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bentley P., Dickinson F. M., Jones I. G. Purification and properties of rabbit muscle L-glycerol 3-phosphate dehydrogenase. Biochem J. 1973 Dec;135(4):853–859. doi: 10.1042/bj1350853. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DALZIEL K. Kinetic studies of liver alcohol dehydrogenase. Biochem J. 1962 Aug;84:244–254. doi: 10.1042/bj0840244. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DALZIEL K. The purification of nicotinamide adenine dinucleotide and kinetic effects of nucleotide impurities. J Biol Chem. 1963 Apr;238:1538–1543. [PubMed] [Google Scholar]
- Gibson Q. H., Milnes L. Apparatus for rapid and sensitive spectrophotometry. Biochem J. 1964 Apr;91(1):161–171. doi: 10.1042/bj0910161. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kim S. J., Anderson B. M. Coenzyme binding to L-alpha-glycerophosphate dehydrogenase. J Biol Chem. 1969 Mar 25;244(6):1547–1551. [PubMed] [Google Scholar]
- VAN EYS J., NUENKE B. J., PATTERSON M. K., Jr The nonprotein component of alpha-glycerophosphate dehydrogenase. Physical and chemical properties of the crystalline rabbit muscle enzyme. J Biol Chem. 1959 Sep;234:2308–2313. [PubMed] [Google Scholar]