通过色谱聚焦法从牛肝中分离纯化线粒体单胺氧化酶B
Isolation and purification of mitochondrial monoamine oxidase B from bovine liver by chromatofocusing.
作者信息
Daya S, Mia R B, Whiteley C G
机构信息
Department of Biochemistry and Microbiology, Rhodes University, Grahamstown Republic of South Africa.
出版信息
Biochem Int. 1992 Jul;27(2):321-33.
Mitochondrial monoamine oxidase B has been isolated and purified from bovine liver. The isolation procedure involves (a) a series of purification steps including isolation of the mitochondria, extraction with non-ionic detergents and chromatofocusing; (b) a novel fluorimetric titration assay. The purified enzyme is isolated following a 8.8 fold purification with an overall yield of 12% and a specific activity of 3460 nM.g-1. A comparison is made with other established procedures. Ion exchange chromatography on DEAE-Cellulose produced a 6.8 fold purification, 6.2% yield and 2383.3 nM.g-1 specific activity while with affinity chromatography on Blue Sepharose CL-6B gave a 3 fold purification, 4.1% yield and a specific activity of 1152.7 nM.g-1.
线粒体单胺氧化酶B已从牛肝中分离纯化出来。分离过程包括：(a) 一系列纯化步骤，包括线粒体的分离、用非离子去污剂提取和色谱聚焦；(b) 一种新型荧光滴定法。纯化后的酶经过8.8倍的纯化，总产率为12%，比活性为3460 nM·g⁻¹。并与其他既定方法进行了比较。在DEAE-纤维素上进行离子交换色谱法得到了6.8倍的纯化，产率为6.2%，比活性为2383.3 nM·g⁻¹；而在蓝色琼脂糖凝胶CL-6B上进行亲和色谱法得到了3倍的纯化，产率为4.1%，比活性为1152.7 nM·g⁻¹。
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