Separation of three P450 isozymes from liver microsomes of gilthead seabream treated with D-NF and partial purification of cytochrome P4501A1

Sen, A
Arinc, E
Three distinct cytochrome P450 isozymes, P4501A1, P4502B and an unidentified P450 isozyme were separated and isolated from beta-NF-treated gilthead seabream liver microsomes. Cytochrome P4501A1 was partially purified from beta-NF-treated gilthead seabream liver microsomes in the presence of detergents Emulgen 913 and cholate and protease inhibitors using two DEAE-cellulose, Porapak Q and two hydroxylapatite column chromatographies. The overall yield of purified P4501A1 was 1.2% with respect to microsomal total P450 with a specific content of 3 nmol/mg protein. The purified P4501A1 was characterized with respect to spectral, electrophoretic, biocatalytic and immunochemical properties, which are found to be similar to P4501A1s purified from other teleost species such as trout, scup, cod and perch suggesting that the P450 we have purified belongs to CYP1A1.


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Acetyl-coenzyme A (AcCoA)-dependent arylamine N-acetyltransferase (NAT:EC was isolated from sheep liver and the specific activity was found as 5.3+/-1.4x10(-3) (mean+/-SE, n=8) nmoles/ min/ mg protein. The effects of p-aminobenzoic acid (PABA) and acetylCoA concentrations, pH, amount of enzyme and reaction period, on the enzyme activity were also studied and the optimum conditions for maximum activity of sheep liver NAT was determined. Sulfamethazine (SMZ) was used as a substrate in order to study ...
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Characterization of proteome alterations in Phanerochaete chrysosporium in response to lead exposure
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Citation Formats
A. Sen and E. Arinc, “Separation of three P450 isozymes from liver microsomes of gilthead seabream treated with D-NF and partial purification of cytochrome P4501A1,” BIOCHEMISTRY AND MOLECULAR BIOLOGY INTERNATIONAL, pp. 131–141, 1997, Accessed: 00, 2020. [Online]. Available: