[Comparison of peptide maps and functional properties of monooxygenases induced by 3-methylcholanthrene and beta-naphthoflavone].
A comparative study revealed a similarity of catalytic, spectral, electrophoretic and immunochemical properties of microsomal cytochromes P-448 (Mr = 56,000) synthesized de novo in 3-methylcholanthrene- and beta-naphthoflavone-treated rats. The identity of peptide maps of microsomal and isolated cytochromes P-448 confirms the validity of the limited proteolysis method for identification of the homogeneity of microsomal hemoproteins and for a comparison of their structures. The data obtained provide a way for evaluation of similarity and differences in the structure and enzymatic activity of various monooxygenase forms without their preliminary isolation from the microsomal membrane.
D000818:Animals; D001571:Benzoflavones / Q000494:pharmacology*; D019388:Cytochrome P-450 CYP1A2; D003580:Cytochromes / Q000032:analysis / Q000096:biosynthesis*; D004790:Enzyme Induction / Q000187:drug effects; D005419:Flavonoids / Q000494:pharmacology*; D008297:Male; D008748:Methylcholanthrene / Q000494:pharmacology*; D008862:Microsomes, Liver / Q000201:enzymology*; D010449:Peptide Mapping; D051381:Rats; D011919:Rats, Inbred Strains; D019324:beta-Naphthoflavone
D001571:Benzoflavones; D003580:Cytochromes; D005419:Flavonoids; D008748:Methylcholanthrene; D019324:beta-Naphthoflavone; C017170:Cyp1a2 protein, rat; D019388:Cytochrome P-450 CYP1A2
Sravnenie peptidnykh kart i funktsional'nykh svoĭstv monooksigenaz, indutsirovannykh 3-metilkholantrenom i beta-naftoflavonom.