文章基本信息

标题：Affinity purification of alkylglycerol monooxygenase from rat liver microsomes by chimyl alcohol-Sepharose 4B column chromatography.
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作者：T Ishibashi ; Y Imai
期刊名称：JLR Papers In Press
印刷版ISSN：0022-2275
电子版ISSN：1539-7262
出版年度：1985
卷号：26
期号：3
页码：393-395
语种：English
出版社：American Society for Biochemistry and Molecular Biology
摘要：Alkylglycerol monooxygenase of rat liver microsomes was purified approximately to 97-fold with a 30% yield by procedures including affinity chromatography on chimyl alcohol-Sepharose 4B. Chimyl alcohol (1-O-hexadecylglycerol) was converted to the p-aminobenzylidene derivative and then coupled to 6-carboxyhexyl-Sepharose. The final enzyme preparation was in nearly a homogeneous state, judging from the results of sodium dodecyl sulfate-polyacrylamide disc gel electrophoresis, and it migrated to a position corresponding to an apparent molecular weight of 45,000. The results revealed that the native form of the enzyme (estimated to have a molecular weight of 400,000 as judged by Sepharose 6B column chromatography in a previous report, Ishibashi, T., and Y. Imai. 1983. Eur. J. Biochem. 132: 23-27) will polymerize to large aggregates.