PMID: 8605221Feb 9, 1996Paper

Purification and properties of a new beta-naphthoflavone inducible cytochrome P-450, aryl hydrocarbon hydroxylase from rat kidney

Biochimica Et Biophysica Acta
N OhgiyaA Yuasa

Abstract

In rat kidney, beta-naphthoflavone induced 53 kDa and 55 kDa proteins, which were both recognized by the antibodies against rat liver cytochrome P-450 1A1 (55kDa). The major inducible 53 kDa protein was purified from the beta naphthoflavone-treated rat kidney and shown to be a new cytochrome P-450 having a high aryl hydrocarbon hydroxylase activity. Purified cytochrome P-450, named P-450KAh, was homogeneous on SDS-polyacrylamide gel electrophoresis, and the apparent molecular weight was estimated to be 53 kDa. The absorption spectra of the oxidized form of P-450KAh showed a Soret peak at 416 nm, a characteristic of low-spin hemoprotein, and the Soret peak of the reduced cytochrome P-450-CO complex was at 446 nm. In the reconstituted system, purified P-450KAh showed high catalytic activity for benzo[a]pyrene hydroxylation and 7-ethoxycoumarin O-deethylation. P-450KAh could activate genotoxicities of not only B[a]P, but also 2-acetylaminofluorene and aflatoxin B1 on the umu test. These catalytic properties of P-450KAh were almost the same as those of P-4501A1, a major P-450 form having arylhydrocarbon hydroxylase in liver microsomes of 3-methylcholanthrene-treated rats, and P-450KAh could not be distinguished from P-4501A1 even b...Continue Reading

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Citations

Nov 14, 2006·Life Sciences·Nagako TanakaHiroshi Yokota

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