Abstract
The specificity of the interaction of cytochrome b5 with different forms of cytochrome P-450 was examined. Immunopurification of cytochromes P-450 1A1, 2B1 and 2E1 from rat liver microsomes resulted in co-purification of cytochrome b5 with cytochrome P-450 forms 2B1 and 2E1 but not 1A1. This specificity was evaluated in conjunction with multiple sequence alignment of the three cytochrome P-450s and a molecular model of the cytochrome P-450-cytochrome b5 complex [(1989) Biochemistry 28, 8201-8205]. These analyses suggest two basic residues in the arginine cluster region of P-450, which are present in P-450s 2B1 and 2E1 but are absent in P-450 1A1, as potential binding sites for cytochrome b5.
MeSH terms
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Amino Acid Sequence
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Animals
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Cytochrome P-450 CYP1A1
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Cytochrome P-450 CYP2B1
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Cytochrome P-450 CYP2E1
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Cytochrome P-450 Enzyme System / chemistry
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Cytochrome P-450 Enzyme System / isolation & purification
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Cytochrome P-450 Enzyme System / metabolism*
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Cytochromes b5 / chemistry
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Cytochromes b5 / isolation & purification
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Cytochromes b5 / metabolism*
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Male
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Microsomes, Liver / enzymology
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Models, Molecular
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Molecular Sequence Data
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Oxidoreductases / chemistry
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Oxidoreductases / isolation & purification
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Oxidoreductases / metabolism
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Oxidoreductases, N-Demethylating / chemistry
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Oxidoreductases, N-Demethylating / isolation & purification
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Oxidoreductases, N-Demethylating / metabolism
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Rats
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Rats, Sprague-Dawley
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Sequence Alignment
Substances
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Cytochromes b5
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Cytochrome P-450 Enzyme System
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Oxidoreductases
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Cytochrome P-450 CYP2E1
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Cytochrome P-450 CYP1A1
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Cytochrome P-450 CYP2B1
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Oxidoreductases, N-Demethylating