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 SpecificityABSTRACT
Serum lipid peroxide levels were estimated in 205 healthy human subjects. The serum lipid peroxide levels in terms of malondialdehyde/ml was 1.47 nmol in male subjects with 11-20 years and which rose to a peak 2.97 in subjects with 51-60 years. Male subjects exhibited significantly higher (P less than 0.01) values as compared to female subjects in whom this increase with age was not observed.