FAD Transport and FAD-dependent Protein Thiol Oxidation in Rat Liver Microsomes
نویسندگان
چکیده
منابع مشابه
FAD transport and FAD-dependent protein thiol oxidation in rat liver microsomes.
The transport of FAD and its effect on disulfide bond formation was investigated in rat liver microsomal vesicles. By measuring the intravesicular FAD-accessible space, we observed that FAD permeates across the microsomal membrane and accumulates in the lumen. Rapid filtration experiments also demonstrated the uptake and efflux of the compound, which could be inhibited by atractyloside and 4,4'...
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A newly discovered human diaphorase, designated diaphorase-4, which accounts for a major part of the diaphorase activity of most tissues but does not occur in erythrocytes, is described. In contrast with other human diaphorases, it is dependent on FAD for activity after electrophoresis, inhibited by low concentrations of dicoumarol and shows a marked affinity for Cibacron Blue. The molecular we...
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The molecular steps of the electron transfer in the endoplasmic reticulum from the secreted proteins during their oxidation are relatively unknown. We present here that flavine adenine dinucleotide (FAD) is a powerful oxidizer of the oxidoreductase system, Ero1 and PDI, besides the proteins of rat liver microsomes and HepG2 hepatoma cells. Inhibition of FAD transport hindered the action of FAD....
متن کاملThe oxidation of hydrazine derivatives catalyzed by the purified liver microsomal FAD-containing monooxygenase.
A number of hydrazine derivatives were tested as substrates for the purified liver microsomal FAD-containing monooxygenase and the kinetic properties of the oxidation reactions were partially characterized. Only 1,l-dimethylhydrazine, l-methyl-l-phenylhydrazine, and the N-aminoheterocyclic hydrazines are oxidized as effectively as N,N-dimethylaniline, one of the best N-methylamine substrates fo...
متن کاملThe FAD Project
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2004
ISSN: 0021-9258
DOI: 10.1074/jbc.m307783200