Purification of NADH-Cytochrome b5 reductase from pig testis microsomes by isoelectric focusing

被引：0
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作者：
Kuwada, M
Hasumi, H
Maki, J
Furuse, Y
机构：
[1] Kitasato Univ, Sch Med, Dept Biochem, Sagamihara, Kanagawa 228, Japan
[2] Kitasato Univ, Sch Med, Dept Biophys Chem, Sagamihara, Kanagawa 228, Japan
[3] Kitasato Univ, Sch Med, Dept Parasitol, Sagamihara, Kanagawa 228, Japan
来源：
BIOCHEMICAL ARCHIVES | 1998年 / 14卷 / 04期
关键词：
D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Testicular NADH-Cytochrome b5 reductase was purified by a procedure including preparative isoelectrofocusing. NADH-Cytochrome b5 reductase was determined to have an isoelectric point of 6.41 on analytical isoelectric focusing. Purified NADH-Cytochrome b5 reductase was found to be homogeneous and its molecular weight was estimated to be 33000 on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. 628-fold purification was achieved with an yield of 15.2%. Following preparation of the microsomes, the purification is accomplished by a two-step procedure utilizing column chromatography and preparative isoelectric focusing.
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页码：247 / 257
页数：11
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