Purification of erythrocyte cytochrome P-450 from goat and chick.
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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Substrate Specificity
/
Goats
/
Kinetics
/
Chickens
/
Chromatography, DEAE-Cellulose
/
Cytochrome P-450 Enzyme System
/
Electrophoresis, Polyacrylamide Gel
/
Erythrocytes
/
Hemolysis
/
Animals
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1992
Type:
Article
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