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Showing 1-25 of 25 results for "T7375" within Papers
ALT reagent with thionicotinamide adenine dinucleotide.
P A Dolan et al.
Clinical chemistry, 35(9), 1857-1858 (1989-09-01)
E F Skorkowski et al.
The International journal of biochemistry, 22(5), 471-475 (1990-01-01)
1. Skeletal muscle mitochondrial NAD(P)-dependent malic enzyme [EC 1.1.1. 39, L-malate:NAD+ oxidoreductase (decarboxylating)] from herring could use both coenzymes, NAD and NADP, in a similar manner. 2. The coenzyme preference of mitochondrial NAD(P)-dependent malic enzyme was probed using dual wavelength
William E Karsten et al.
Biochemistry, 41(40), 12193-12199 (2002-10-03)
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. pH-rate profiles and isotope effects were
TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes
Essuman K, et al.
Current Biology, 28(3), 421-430 (2018)
Circular dichroic properties and conformation of thionicotinamide dinucleotides
European Journal of Biochemistry, 83(2), 587-592 (1978)
K B Male et al.
The International journal of biochemistry, 14(12), 1083-1089 (1982-01-01)
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 NAD. 2. S-NAD
S Alex et al.
The Biochemical journal, 191(2), 299-304 (1980-11-01)
The thionicotinamide analogues of NAD+ and NADP+ were shown to be good alternative coenzymes for bovine glutamate dehydrogenase, with similar affinity and approx. 40% of the maximum velocity obtained with the natural coenzymes. Both thionicotinamide analogues show non-linear Lineweaver-Burk plots
P H Pekala et al.
Molecular and cellular biochemistry, 31(1), 49-56 (1980-05-28)
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 observed with intact cells, ghosts and solubilized enzyme and
J D Hermes et al.
Biochemistry, 23(23), 5479-5488 (1984-11-06)
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 effects in formate
[Simultaneous assay of serum lactate dehydrogenase activities depending on NAD (N) and thio-NAD (T), and the clinical significance of N/T values].
M Kawai
Nihon Shokakibyo Gakkai zasshi = The Japanese journal of gastro-enterology, 83(11), 2458-2458 (1986-11-01)
D M Kiick et al.
Biochemistry, 25(1), 227-236 (1986-01-14)
The pH dependence of the kinetic parameters and the primary deuterium isotope effects with nicotinamide adenine dinucleotide (NAD) and also thionicotinamide adenine dinucleotide (thio-NAD) as the nucleotide substrates were determined in order to obtain information about the chemical mechanism and
J R Florini
Analytical biochemistry, 182(2), 399-404 (1989-11-01)
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
Suppression of cytosolic NADPH pool by thionicotinamide increases oxidative stress and synergizes with chemotherapy
Tedeschi PM, et al.
Molecular Pharmacology, 88(4), 720?727-720?727 (2015)
Simultaneous determination of multiple forms of lactate dehydrogenase based on NAD and thio-NAD.
S Hosaki et al.
Clinica chimica acta; international journal of clinical chemistry, 157(3), 321-322 (1986-06-30)
NAD+ kinase as a therapeutic target in cancer
Tedeschi PM, et al.
Clinical Cancer Research, 22(21), 5189-5195 (2016)
Gregory Yakovlev et al.
Biochemistry, 46(49), 14250-14258 (2007-11-16)
NADH-ubiquinone oxidoreductase (complex I) is the first enzyme of the respiratory electron transport chain in mitochondria. It conserves the energy from NADH oxidation, coupled to ubiquinone reduction, as a proton motive force across the inner membrane. Complex I catalyzes NADPH
Comparative kinetics of cofactor association and dissociation for the human and trypanosomal S-adenosylhomocysteine hydrolases. 1. Basic features of the association and dissociation processes
Li QS, et al
Biochemistry, 46(19), 5798-5809 (2007)
Shigeru Ueda et al.
Analytical biochemistry, 332(1), 84-89 (2004-08-11)
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-HSD) with nucleotide cofactors, thio-NAD(+) (one of the
A Argyrou et al.
Biochemistry, 40(38), 11353-11363 (2001-09-19)
The gene encoding dihydrolipoamide dehydrogenase from Mycobacterium tuberculosis, Rv0462, was expressed in Escherichia coli and the protein purified to homogeneity. The 49 kDa polypeptide forms a homodimer containing one tightly bound molecule of FAD/monomer. The results of steady-state kinetic analyses
H H Ting et al.
The Biochemical journal, 215(2), 361-368 (1983-11-01)
Bovine lens cytoplasmic aldehyde dehydrogenase exhibits Michaelis-Menten kinetics with acetaldehyde, glyceraldehyde 3-phosphate, p-nitrobenzaldehyde, propionaldehyde, glycolaldehyde, glyceraldehyde, phenylacetylaldehyde and succinic semialdehyde as substrates. The enzyme was also active with malondialdehyde, and exhibited an esterase activity. Steady-state kinetic analyses show that the
R M Burger et al.
The Journal of biological chemistry, 260(29), 15406-15409 (1985-12-15)
Activated bleomycin appears to have two more oxidizing equivalents than the Fe(III).bleomycin to which it spontaneously decays. Activated bleomycin reacts with NADH and thio-NADH, two-electron reductants, and with KI, a one-electron reductant, to yield Fe(III).bleomycin. The observed stoichiometries were 0.85
Kinetic studies of multifunctional reactions catalysed by lipoamide dehydrogenase.
C S Tsai
The International journal of biochemistry, 11(5), 407-413 (1980-01-01)
P M Weiss et al.
Biochemistry, 30(23), 5755-5763 (1991-06-11)
Deuterium isotope effects and 13C isotope effects with deuterium- and protium-labeled malate have been obtained for both NAD- and NADP-malic enzymes by using a variety of alternative dinucleotide substrates. With nicotinamide-containing dinucleotides as the oxidizing substrate, the 13C effect decreases
B M Anderson et al.
Archives of biochemistry and biophysics, 321(1), 94-100 (1995-08-01)
Azotobacter vinelandii glucose-6-phosphate dehydrogenase isolated from cell sonicates was purified 81-fold to electrophoretic homogeneity and a specific activity of 73 units/mg protein using ion-exchange and Matrex Dye chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and molecular exclusion chromatography indicated the enzyme
R A Laun et al.
Clinical and experimental medicine, 1(4), 201-209 (2002-03-29)
The arterial ketone body ratio is calculated as the ratio of arterial levels of acetoacetate/beta-hydroxybutyrate. It correlates with survival in experimental hemorrhagic shock and outcome after liver surgery and myocardial infarction. Procedures for determination of ketone bodies are often laborious
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