Purification of NADPH-Cytochrome P-450 Reductase from Pig Testis Microsomes by Isoelectric Focusing in an Immobiline pH Gradient
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概要
- 論文の詳細を見る
Testicular NADPH-Cytochrome P-450 reductase was purified by a procedure including preparative isoelectrofocusing. NADPH-Cytochrome P-450 reductase was determined to have an isoelectric point of 5.35 on analytical isoelectric focusing. Purified NADPH-Cytochrome P-450 reductase was found to be homogeneous and its molecular weight was estimated to be 78000 on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The spectrum of the oxidized form was that of a typical flavoprotein with absorption peak at 380 and 454nm. 1144-fold purification was achieved with a yield of 3.69%. Following preparation of the microsomes, the purification is accomplished by a two-step procedure utilizing column chromatography and preparative isoelectric focusing.
- 北里大学の論文
- 1998-08-31
著者
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Furuse Yuko
Department of Radioisotope Center, Kitasato University School of Medicine
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Furuse Yuko
Department Of Biochemistry Kitasato University School Of Medicine
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KUWADA Masahiro
Department of Biochemistry, Kitasato University School of Medicine
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HASUMI Hideo
Department of Biophysical Chemistry, School of Medicine, Kitasato University
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Hasumi H
Kitasato Univ. Kanagawa Jpn
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Hasumi Hideo
Department Of Biophysical Chemistry School Of Medicine Kitasato University
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Kuwada Masahiro
Department Of Biochemistry Kitasato University School Of Medicine
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