Characterization of two P-450 isozymes placed in the rat CYP2D subfamily

• Published in: Biochimica et biophysica acta Vol. 1158; no. 3; pp. 227 - 236
• Main Authors: Ohishi, Norihisa, Imaoka, Susumu, Suzuki, Tokuji, Funae, Yoshihiko
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 28.11.1993; Elsevier
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Antibodies - pharmacology; Biological and medical sciences; CYP2D; Cytochrome P-450; Cytochrome P-450 CYP2D6; Cytochrome P-450 Enzyme Inhibitors; Cytochrome P-450 Enzyme System - chemistry; Cytochrome P-450 Enzyme System - isolation & purification; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Isoenzymes - chemistry; Lidocaine - metabolism; Male; Microsomes, Liver - enzymology; Mixed Function Oxygenases - antagonists & inhibitors; Mixed Function Oxygenases - chemistry; Mixed Function Oxygenases - isolation & purification; Molecular Sequence Data; Oxidoreductases; rat hepatic microsomes; Rats; Rats, Sprague-Dawley; lidocaine metabolism; rat hepatic microsomes; CYP2D; Cytochrome P-450; Vertebrata; Mammalia; Purification; Hydroxylation; Rat; Isozyme; Cytochrome P450; Liver; Rodentia; Microsome; Physicochemical properties

Two P-450s with debrisoquine 4-hydroxylation activity, designated P-450 UT-7 and UT-7b, were purified and partially purified, respectively, from hepatic microsomes of untreated male rats. Both purified P-450s with an apparent molecular weight of 49 000, were associated with another protein with an a...