%0 Journal Article
%T Purification of monoamine oxidase B from porcine liver<br>猪肝中单胺氧化酶B的分离纯化
%A SUN Jiayi
%A REN Jun
%A XU Li
%A JIA Lingyun
%A <br>孙嘉怡
%A 任军
%A 徐丽
%A 贾凌云
%J 色谱
%D 2010
%I 
%X Monoamine oxidase B (MAOB) was purified from porcine liver by solubilization with lysis buffer containing 1% Triton X-100, precipitation with 20%~50% ammonium sulfate, isolation with hydrophobic chromatography and anion exchange chromatography. The purification fold was 18.2. The specific activity was 135 U/mg. The purified enzyme appeared homogeneous by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and it had a relative molecular mass of about 60 000. The identification of the enzyme was confirmed by high performance liquid chromatography-electrospray ionization tandem mass spectrometry (HPLC-ESI-MS/MS). As MAOB is a membrane enzyme, a key step to the successful purification was the use of Phenyl-Sepharose CL-4B with phenyl density of 75.7 μmol/mL. The results showed that this approach could effectively isolate MAOB from porcine liver to yield an enzyme with high purity and specific activity.
%K phenyl ligand
%K hydrophobic chromatography
%K anion exchange chromatography
%K monoamine oxidase B
%K porcine liver<br>苯基配基
%K 疏水色谱
%K 阴离子交换色谱
%K 单胺氧化酶B
%K 猪肝
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=6E709DC38FA1D09A4B578DD0906875B5B44D4D294832BB8E&cid=6579068328FE643F&jid=4D81E042D77AFEC6881D14759692069C&aid=1F617D3CADF2CE05916683AC4FF67703&yid=140ECF96957D60B2&vid=D3E34374A0D77D7F&iid=9CF7A0430CBB2DFD&sid=11632AEF1E1F2092&eid=BE05E2A2B7E55AA9&journal_id=1000-8713&journal_name=色谱&referenced_num=0&reference_num=13