Monoclonal antibody directed isolation and amino-terminal sequence analysis of phenobarbital induced rat liver cytochromes P-450.
Cytochrome P-450 was isolated from liver microsomes of phenobarbital treated rats by an essentially single step immunopurification with a monoclonal antibody (MAb). The amino terminal sequence of the isolated cytochrome P-450 displayed a microheterogeneity of isozymes related to previously identified phenobarbital induced forms, indicating that each of these isozymes possess the MAb-specific epitope. This monoclonal antibody-based approach to isolation and subsequent identification of cytochrome P-450 may serve to classify different isozymes by their content of epitopes that bind to different MAbs.
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D002846:Chromatography, Affinity; D003577:Cytochrome P-450 Enzyme System / Q000096:biosynthesis / Q000302:isolation & purification*; D004790:Enzyme Induction; D007527:Isoenzymes / Q000096:biosynthesis / Q000302:isolation & purification*; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D010634:Phenobarbital / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains
D000911:Antibodies, Monoclonal; D007527:Isoenzymes; D003577:Cytochrome P-450 Enzyme System; D010634:Phenobarbital