Direct Enzyme Titration Curve of NADH: Cytochrome b5 Reductase by Combined Isoelectric Focusing/Electrophoresis. Interactions between Enzyme and Cytochrome b5

Unusual dehydroxylation of antimicrobial amidoxime prodrugs by cytochrome b5 and NADH cytochrome b5 reductase.

Furamidine is an effective antimicrobial agent; however, oral potency of furamidine is poor. A prodrug of furamidine, 2,5-bis(4-amidinophenyl)furan-bis-O-methylamidoxime (DB289), has greatly improved oral potency. DB289 is transformed to furamidine via O-demethylation, and N-dehydroxylation reactions with four intermediate metabolites formed. The O-demethylation reactions have been shown to be ...

Unusual Dehydroxylation of Antimicrobial Amidoxime Prodrugs by Cytochrome b5 and NADH Cytochrome b5 Reductase a

The interaction of NADH-cytochrome b5 reductase and cytochrome b5 bound to egg lecithin liposomes.

Incubation of liposomes prepared by sonication of egg lecithin with the amphipathic form of cytochrome b5 results in the binding of a maximum of 244 molecules of cytochrome b5 per liposomal vesicle. Interactions of the phospholipid with the hydrophobic segment of cytochrome b5 are involved in this binding which does not disrupt the liposome. When a small amount of NADH-cytochrome b5 reductase i...

Interaction of non-myristoylated NADH-cytochrome b5 reductase with cytochrome b5-dimyristoylphosphatidylcholine vesicles.

An expression vector for NADH-cytochrome b5 reductase containing a thrombin cleavage site directly before the N-terminal glycine residue of the flavoprotein was used to isolate the non-myristoylated enzyme by thrombin cleavage of the initial fusion protein of a short segment of the multiple cloning site of the plasmid vector and the reductase. This flavoprotein preparation, containing only the ...

Characterization of the purified NADH-cytochrome b5 reductase of human erythrocytes as a FAD-containing enzyme.

NADH-cytochrome b5 reductase of normal human erythrocytes was purified by procedures including affinity chromatography on Blue-Sepharose to an electrophoretically homogeneous protein. The purified enzyme was judged to be a typical flavoprotein based on its absorption spectrum (absorption maxima, 272, 390, and 462 nm; shoulders, 373 and 488 nm) and flavin content (1 mol of FAD/mol of enzyme). Th...