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Comparative Study
. 1987 Jun 26:397:123-36.
doi: 10.1016/s0021-9673(01)84995-5.

Structural comparison between the trout and mammalian hydrophilic domain of NADPH-cytochrome P-450 reductase

J Urenjak  1 , D Linder, L Lumper
Affiliations
Comparative Study

Structural comparison between the trout and mammalian hydrophilic domain of NADPH-cytochrome P-450 reductase

J Urenjak et al. J Chromatogr. .

Abstract

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.

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