[Purification and characteristics of highly active NADPH-cytochrome P-450 reductase from liver microsomes of phenobarbital-induced rabbits].
Liver microsomal NADPH-cytochrome P-450 reductase from phenobarbital-induced rabbits was purified by a simple and reproducible method employing combination of 2',5'-ADP-sepharose affinity chromatography and 1-amino-2-hydroxypropyl-sepharose (ADP-sepharose) ion exchange chromatography. Comparison with traditionally used adsorbents revealed advantages of AHP-sepharose for isolation of highly active enzyme preparations. The enzyme was purified 408-fold with a 92% yield of the total activity. Electrophoretic and spectral properties of the preparation corresponded to those of native flavoprotein. The specific NADPH-cytochrome c reductase activity of the purified enzyme (85.7 U/mg at pH 7.7 and 30 degrees C) was 1.5-2.5 times higher than that previously reported.
Skorostetskaia
L A
LA
Gilevich
S N
SN
D000818:Animals; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004790:Enzyme Induction; D008862:Microsomes, Liver / Q000201:enzymology*; D009251:NADPH-Ferrihemoprotein Reductase / Q000096:biosynthesis / Q000302:isolation & purification*; D010634:Phenobarbital / Q000494:pharmacology*; D011817:Rabbits
D009251:NADPH-Ferrihemoprotein Reductase; D010634:Phenobarbital
Ochistka i kharakteristika vysokoaktivnoŏ NADPH-tsitokhrom-P-450- reduktazy iz mikrosom pecheni krolikov, indutsirovannykh fenobarbitalom.