Purification of cytochrome P450 from filamentous fungus Rhyzopus nigricans

It has been reported in our previous studies that steroid hydroxylation system of Rhizopus nigricans involves cytochrome P450 and NADPH-cytochrome P450 reductase in the electron transport system. Both enzymes are membrane bound and are located in the microsomal preparations of progesterone induced f...

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Bibliographic Details
Published inPflügers Archiv Vol. 439; no. 3 Suppl; pp. R111 - R112
Main Authors Makovec, T, Breskvar, K
Format Journal Article
LanguageEnglish
Published Germany 2000
Subjects
Chromatography, Ion Exchange
Cytochrome P-450 Enzyme System - isolation & purification
Ketoconazole - pharmacology
NADH, NADPH Oxidoreductases - analysis
NADPH-Ferrihemoprotein Reductase
Rhizopus - enzymology
Steroid Hydroxylases - analysis
Subcellular Fractions - enzymology
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Summary:It has been reported in our previous studies that steroid hydroxylation system of Rhizopus nigricans involves cytochrome P450 and NADPH-cytochrome P450 reductase in the electron transport system. Both enzymes are membrane bound and are located in the microsomal preparations of progesterone induced fungal mycelia. In order to identify and characterize the cytochrome P450 component of fungal monoxygenase system, microsomal proteins from induced mycelia were subjected to HIGH Q anion exchange and MONO P (FPLC) anion exchange chromatography. Four fractions containing cytochrome P450 have been resolved on MONO P column. They exhibit CO difference spectra and type II difference spectra with ketoconazole.
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ISSN:0031-6768