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Collagenolytic activity of rabbit V2-carcinoma growing at multiple sites.
Authors:C Biswas  W P Moran  K J Bloch  J Gross
Affiliation:Faculty of Pharmaceutical Sciences, Mukogawa University, Nishinomiya, Hyogo 663, Japan
Abstract:Interaction between lanosterol and cytochrome P-450 purified from microsomes of anaerobically-grown Saccharomyces cerevisiae was studied. Lanosterol (4,4,14α-trimethyl-5α-cholesta-8,24-dien-3β-ol) stimulated the oxidation of NADPH by molecular oxygen in the presence of cytochrome P-450 and NADPH-cytochrome P-450 reductase both purified from S. cerevisiae microsomes. Lanosterol stimulated the reduction of cytochrome P-450 by NADPH with the cytochrome P-450 reductase, and induced Type I spectral change of cytochrome P-450. These observations suggest that lanosterol interacts to the substrate region of cytochrome P-450 of S. cerevisiae. Based on these facts, possible role of cytochrome P-450 in lanosterol metabolism in yeast cell is discussed.
Keywords:Correspondences should be adressed to this author: Yuzo Yoshida Faculty of Pharmaceutical Sciences   Mukogawa University 4-16 Edagawa-cho   Nishinomiya   Hyogo 663   Japan
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