酰胺腺嘌呤二核苷酸(氧化型)
酰胺腺嘌呤二核苷酸(氧化型)结构式
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常用名 | 酰胺腺嘌呤二核苷酸(氧化型) | 英文名 | Thionicotinamide adenine dinucleotide |
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| CAS号 | 4090-29-3 | 分子量 | 679.491 | |
| 密度 | N/A | 沸点 | N/A | |
| 分子式 | C21H27N7O13P2S | 熔点 | N/A | |
| MSDS | 中文版 美版 | 闪点 | N/A |
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Self-inactivation of an erythrocyte NAD glycohydrolase.
Mol. Cell Biochem. 31(1) , 49-56, (1980) NAD glycohydrolase activity was studied using bovine erythrocytes, erythrocyte ghosts and partially purified enzyme preparations. During catalysis the enzyme becomes irreversibly inactivated in a process related to substrate turnover. Self-inactivation was ob... |
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Kinetic study of the enzymatic cycling reaction conducted with 3alpha-hydroxysteroid dehydrogenase in the presence of excessive thio-NAD(+) and NADH.
Anal. Biochem. 332(1) , 84-9, (2004) We have established a simple kinetic model applicable to the enzyme cycling reaction for the determination of 3alpha-hydroxysteroids. This reaction was conducted under the reversible catalytic function of a single 3alpha-hydroxysteroid dehydrogenase (3alpha-H... |
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Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of D-malate with both NAD and thio-NAD.
Biochemistry 41(40) , 12193-9, (2002) Tartrate dehydrogenase catalyzes the divalent metal ion- and NAD-dependent oxidative decarboxylation of D-malate to yield CO(2), pyruvate, and NADH. The enzyme also catalyzes the metal ion-dependent oxidation of (+)-tartrate to yield oxaloglycolate and NADH. ... |
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Simultaneous determination of multiple forms of lactate dehydrogenase based on NAD and thio-NAD.
Clin. Chim. Acta 157(3) , 321-2, (1986)
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ALT reagent with thionicotinamide adenine dinucleotide.
Clin. Chem. 35(9) , 1857-8, (1989)
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[Simultaneous assay of serum lactate dehydrogenase activities depending on NAD (N) and thio-NAD (T), and the clinical significance of N/T values].
Nihon Shokakibyo Gakkai Zasshi 83(11) , 2458, (1986)
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Kinetic studies of multifunctional reactions catalysed by lipoamide dehydrogenase.
Int. J. Biochem. 11(5) , 407-13, (1980)
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Regulation of coenzyme utilization by bovine liver glutamate dehydrogenase: investigations using thionicotinamide analogues of NAD and NADP in a dual wavelength assay.
Int. J. Biochem. 14(12) , 1083-9, (1982) 1. The coenzyme preference of bovine liver glutamate dehydrogenase (GDH) was probed using dual wavelength spectroscopy and pairing the thionicotinamide analogues, S-NAD or S-NADP (which have absorbance maxima at 400 nm), with the natural coenzymes, NADP or NA... |
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Assay of creatine kinase in microtiter plates using thio-NAD to allow monitoring at 405 nM.
Anal. Biochem. 182(2) , 399-404, (1989) An assay system for creatine kinase using microtiter plates and a plate reader that records absorbancies at 405 nM has been devised. The system is an adaptation of well-established assays that couple creatine kinase with the reactions catalyzed by hexokinase ... |
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Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 2. Formate dehydrogenase.
Biochemistry 23(23) , 5479-88, (1984) Since hydride transfer is completely rate limiting for yeast formate dehydrogenase [Blanchard, J.S., & Cleland, W. W. (1980) Biochemistry 19, 3543], the intrinsic isotope effects on this reaction are fully expressed. Primary deuterium, 13C, and 18O isotope ef... |