Purification of erythrocyte cytochrome P-450 from goat and chick.
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.
Patil
S S
SS
Chemistry Department, S.B.E.S. Science College, Aurangabad.
Makhija
S J
SJ
Pawar
S S
SS
D000818:Animals; D002645:Chickens; D002848:Chromatography, DEAE-Cellulose; D003577:Cytochrome P-450 Enzyme System / Q000097:blood* / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D006041:Goats; D006461:Hemolysis; D007700:Kinetics; D008970:Molecular Weight; D013379:Substrate Specificity
D003577:Cytochrome P-450 Enzyme System