Structural comparison between the trout and mammalian hydrophilic domain of NADPH-cytochrome P-450 reductase.
The isolation of the protease-solubilized NADPH-cytochrome P-450 reductase from trout liver and its properties are described. The sequence of the "hydrophilic domain" [protease-solubilized NADPH-cytochrome P-450 reductase from trout (residues Lys56-Ser678)] is reported. The CNBr fragments of the trout "hydrophilic domain" and their proteolytic subpeptides were sequenced. The CNBr fragments were aligned by homology to the reported sequence of the porcine NADPH-cytochrome P-450 reductase. The structures of the mammalian and the trout NADPH-cytochrome P-450 reductases were compared. Stretches with high exchange rates between the pig and trout reductase were found at the NH2 and the COOH terminal regions of the hydrophilic domain.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003488:Cyanogen Bromide; D008099:Liver / Q000201:enzymology; D009251:NADPH-Ferrihemoprotein Reductase / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000032:analysis; D051381:Rats; D012487:Salmonidae / Q000378:metabolism*; D013045:Species Specificity; D013552:Swine; D009626:Terminology as Topic; D014337:Trout / Q000378:metabolism*; D014357:Trypsin
D000596:Amino Acids; D010446:Peptide Fragments; D009251:NADPH-Ferrihemoprotein Reductase; D014357:Trypsin; D003488:Cyanogen Bromide