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Indian J Biochem Biophys ; 1992 Dec; 29(6): 516-8
Article in English | IMSEAR | ID: sea-27723

ABSTRACT

Cytochrome P-450 has been purified from goat and chick erythrocytes and characterized. Goat erythrocyte cytochrome P-450 content was higher than that of chick erythrocytes cytochrome P-450. Elution profile of purified protein from DEAE-cellulose column showed a single peak. The catalytic activities of aminopyrine-N-demethylase and acetanilide hydroxylase were found to be higher in purified proteins. Molecular weight was determined by SDS-polyacrylamide gel electrophoresis.


Subject(s)
Animals , Chickens , Chromatography, DEAE-Cellulose , Cytochrome P-450 Enzyme System/blood , Electrophoresis, Polyacrylamide Gel , Erythrocytes/enzymology , Goats , Hemolysis , Kinetics , Molecular Weight , Substrate Specificity
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