Crystallization of Nicotinamide Adenine Dinucleotide

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Substituted Nicotinamide Analogues of Nicotinamide Adenine Dinucleotide.

A number of nicotinamide adenine dinucleotide analogues have been prepared in which the purine, pyridine, and ribose moieties have been modified (2-12). These analogues have proven to be valuable in studies dealing with the site of binding of the pyridine coenzyme to dehydrogenases, in elucidating the mechanism of dehydrogenases and the configuration of the pyridme coenzymes, and as indicators ...

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Substituted Nicotinamide Analogues of Nicotinamide Adenine Dinucleotide*

A number of nicotinamide adenine dinucleotide analogues have been prepared in which the purine, pyridine, and ribose moieties have been modified (2-12). These analogues have proven to be valuable in studies dealing with the site of binding of the pyridine coenzyme to dehydrogenases, in elucidating the mechanism of dehydrogenases and the configuration of the pyridme coenzymes, and as indicators ...

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

As part of an investigation of the growth of tomato plants supplied with either nitrate or ammonium nitrogen (6), leaves were assayed for NAD4 and NADP. Anderson and Vennesland (1) assayed NAD and NADP in various green tissues and reported recoveries between 50 % and 85 % of NAD and NADP added to spinach leaf extracts. Very low levels of NAD and NADP were recorded for tomato leaf extracts. Thes...

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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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Inhibition of nicotinamidase by nicotinamide adenine dinucleotide.

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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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1964

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)97765-3