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 Lys 56—Ser 678)] is reported. The CNBr fragments of the t...

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Bibliographic Details
Published in:Journal of Chromatography A 1987-06, Vol.397, p.123-136
Main Authors: Urenjak, Jutta, Linder, Dietmar, Lumper, Ludwig
Format: Article
Language:English
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Summary: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 Lys 56—Ser 678)] 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 NH 2 and the COOH terminal regions of the hydrophilic domain.
ISSN:0021-9673
DOI:10.1016/S0021-9673(01)84995-5