Inhibition of Rat Liver Nicotinamide Adenine Dinucleotide Kinase by Reduced Nicotinamide Adenine Dinucleotide Phosphate

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Inhibition of rat liver nicotinamide adenine dinucleotide kinase by reduced nicotinamide adenine dinucleotide phosphate.

Rat liver NAD kinase (ATP : NAD 2’-phosphotransferase, EC 2.7.1.23) was purified about 70-fold. The MichaelisMenten constants (Km) for NAD and ATP were 8 x 10e4 M and 2 x low3 M, respectively. NAD kinase activity was markedly inhibited by NADH and also NADPH. The Ki of NADH was approximately 1 X 10q4 M, and that of NADPH was approximately 5 X 10M5 M. Both inhibitions were competitive with NAD, ...

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Feedback inhibition by NAD was shown with the nicotinamidases of a number of microorganisms. The purified enzyme from Fleischmann’s yeast was found to have a molecular weight of 110,000 and consist of presumably identical subunits with a molecular weight of 26,000. A LineweaverBurk plot of the NAD inhibition is concave upward at low concentrations of NAD; at 6 mr+r NAD, the linear plot is that ...

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Measurement of nicotinamide adenine dinucleotide & nicotinamide adenine dinucleotide phosphate in tomato leaves.

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1968

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)81738-6