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NAD +

Keita B, Nad]o L and K]oller K 1991 Surface characterization of a single crystal of sodium decatungstocerate (IV) by the atomic force microscope Surf. Sc/. Lett. 256 L613... [Pg.1726]

FIGURE 15 5 Structure of NAD the oxidized form of the coenzyme nicotinamide adenine dinucleotide The functional part of the coen zyme is framed in red... [Pg.646]

The reverse reaction also occurs m living systems NADH reduces acetaldehyde to ethanol m the presence of alcohol dehydrogenase In this process NADH serves as a hydride donor and is oxidized to NAD" while acetaldehyde is reduced... [Pg.646]

The NAD -NADH coenzyme system is involved m a large number of biological changes during the enzyme... [Pg.647]

IS the oxidation of lactic acid to pyruvic acid by NAD and the enzyme lactic acid coenzyme NAD ... [Pg.647]

We shall encounter other biological processes m which the NAD" conversion plays a prominent role m biological oxidation-reduction... [Pg.647]

Section 15 11 Oxidation of alcohols to aldehydes and ketones is a common biological reaction Most require a coenzyme such as the oxidized form of nicotin amide adenine dmucleotide (NAD" )... [Pg.655]

All the individual steps are catalyzed by enzymes NAD" (Section 15 11) is required as an oxidizing agent and coenzyme A (Figure 26 16) is the acetyl group acceptor Coen zyme A is a thiol its chain terminates m a sulfhydryl (—SH) group Acetylation of the sulfhydryl group of coenzyme A gives acetyl coenzyme A... [Pg.1070]

Cortisol-Cortisone Conversion. Under normal conditions, this equilibrium slightly favors the oxidized compound. Similarly, the conversion of corticosterone to 11-deoxycorticosterone is also mediated by the liP-hydroxysteroid dehydrogenase enzyme system and requites NAD(P) /NAD(P)H. This conversion is especially important both in the protection of the human fetus from excessive glucocorticoid exposure, and in the protection of distal nephron mineral ocorticoid receptors from glucocorticoid exposure (14). The impairment of this conversion is thought to result in hypertension associated with renal insufficiency (15). [Pg.97]

J. W. Hastie and D. W. BonneU, Molecular Chemist of Inhibited Combustion Systems, Feport NBSIF 80-2169, Nad. Buieau of Standards, Washington, D.C., 1980. [Pg.482]

Standardfor FiquifiedHydrogen Systems at Consumer Sites, Nad. Eke Protect. Assoc, pamphlet no. 50B (ANSI Z292.3), 1973. [Pg.436]

Insects poisoned with rotenone exhibit a steady decline ia oxygen consumption and the iasecticide has been shown to have a specific action ia interfering with the electron transport iavolved ia the oxidation of reduced nicotinamide adenine dinucleotide (NADH) to nicotinamide adenine dinucleotide (NAD) by cytochrome b. Poisoning, therefore, inhibits the mitochondrial oxidation of Krebs-cycle iatermediates which is catalysed by NAD. [Pg.270]


See other pages where NAD + is mentioned: [Pg.155]    [Pg.176]    [Pg.269]    [Pg.274]    [Pg.274]    [Pg.274]    [Pg.274]    [Pg.238]    [Pg.414]    [Pg.297]    [Pg.139]    [Pg.192]    [Pg.344]    [Pg.645]    [Pg.645]    [Pg.645]    [Pg.645]    [Pg.646]    [Pg.647]    [Pg.647]    [Pg.684]    [Pg.735]    [Pg.1070]    [Pg.1147]    [Pg.539]    [Pg.673]    [Pg.673]    [Pg.476]    [Pg.29]    [Pg.293]    [Pg.512]    [Pg.26]    [Pg.26]    [Pg.273]    [Pg.273]   
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See also in sourсe #XX -- [ Pg.9 , Pg.17 , Pg.61 , Pg.63 , Pg.89 ]




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ADH-NAD (

Absorption spectra of NAD+

Biomimetic reduction NAD H models

Carba-NAD

Catabolism of NAD (P)

Coenzyme NAD

Cofactor NAD H

Cyanide ion adduct with NAD

D-Glyceraldehyde-3-phosphate:NAD

Deamido NAD

Dehydrogenases NAD binding structure

Dehydrogenases NAD+ linked

Desamido NAD

Dextran-NAD

Electrochemical Regeneration of NAD(P)H

Enzyme-bound NAD

Ferredoxin-NAD oxidoreductase

Ferredoxin-NAD reductase

Generation in situ of NAD by Grafting Reactions

Gibbs energy by NAD+, table

Glucose 6-phosphate-NAD

L-Glutamate:NAD oxidoreductase

L-Lactate: NAD oxidoreductase

L-Malate:NAD oxidoreductase

Mechanism of the Reduction with NAD(P)H Models

Model Reactions of NAD(P)H-Dependent Dehydrogenases

NAD (p-Nicotinamide

NAD + nucleosidase

NAD +-dependent dehydrogenases

NAD +-dependent enzymes

NAD -dependent dehydrogenase

NAD H

NAD H dehydrogenase

NAD Pyrophosphorylase

NAD Recycling

NAD and NADH

NAD and NADP systems

NAD binding

NAD biosynthesis

NAD catabolism

NAD complexes

NAD dependent oxidoreductases

NAD erythrocytes

NAD function

NAD glycohydrolase

NAD glycohydrolase inhibitors

NAD intracellular concentration

NAD kinase

NAD kynureninase

NAD kynurenine hydroxylase

NAD metabolism

NAD oxidation

NAD picolinate carboxylase

NAD polymerization

NAD pyrophosphatase

NAD redox functions

NAD reductase

NAD synthesis

NAD synthetase

NAD transhydrogenase

NAD tryptophan

NAD tryptophan dioxygenase

NAD(P) Biosynthesis

NAD(P)-linked enzymic oxidations

NAD(P)H Oxidase

NAD(P)H-Alcohol Dehydrogenase Substrates

NAD* containing

NAD* determination

NAD* radical

NAD+ and NADP

NAD+ as coenzyme

NAD+ as oxidizing agent

NAD+ hydrolysis

NAD+ reduction

NAD+ regeneration

NAD+ structure

NAD+, NADP

NAD+, hydrogenation

NAD+-dependent deacetylases

NAD+-glycohydrolysis

NAD+/NADH balance

NAD+/NADH redox couple

NAD, NADH, NADP

NAD, NADH, NADP, NADPH

NAD, depletion

NAD-Dependent Deacetylases as Therapeutic Targets

NAD-Dependent HDAC Modulators

NAD-Dependent Malate Dehydrogenases

NAD-Dependent Oxidation of Ethanol

NAD-binding fold

NAD-dependent dehydrogenation

NAD-dependent glucose dehydrogenase

NAD-dependent malic enzyme

NAD-dependent substrate oxidation

NAD-linked hydrogenase

NAD-malic enzyme

NAD/NADH

NADH, reduced NAD

NADH/NAD ratio

NADPH, reduced NAD

NADPH:NAD transhydrogenase

NADS, National Advanced Driving Simulator

NAD—See Nicotinamide adenine

NAD—See Nicotinamide adenine dinucleotide

NO-Stimulated NAD-Dependent Modification of GAPDH

Nicotinamide Adenine Dincleotide (NAD)

Nicotinamide adenine dinucleotide (NAD,NADH

Nicotinamide adenine dinucleotide phosphate (NAD

Nicotinamide adenine dinucleotide. See NAD*, NADH

Nicotinamide adenine dinucleotides NAD/NADH)

Nicotinamide adenosine dinucleotide (NAD

Nicotinamide cofactors NAD

Non aqueous dispersions (NAD

Oxidation of Ethanol by NAD

Reduction NAD H model compounds

Reductions of NAD

Regeneration of NAD

Roles for NAD(P)H Oxidases as Vascular Oxygen Sensors and Their Influence on Oxidant-Regulated Signaling Mechanisms

Subcellular Compartmentation of NAD and Its Metabolism

Succinate-linked NAD+ reduction

The Electrical Contacting of NAD(P)-dependent Enzymes

The NAD Reduced in Glycolysis Must Be Regenerated

The Redox Function of NAD (P)

Thio-NAD

Use of NAD (P) in Enzyme Assays

Vitamin NAD glycohydrolase inhibitor

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