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通过区带超速离心法纯化载脂蛋白-胆汁脂蛋白复合物的人阴离子多肽组分。

Purification of the human anionic polypeptide fraction of the apo-bile lipoprotein complex by zonal ultracentrifugation.

作者信息

Martigne M, Domingo N, Lafont H, Nalbone G, Hauton J C

出版信息

Lipids. 1985 Dec;20(12):884-9. doi: 10.1007/BF02534772.

Abstract

The two main proteic constituents of the human Apo-bile lipoprotein complex (BLC), i.e., the anionic polypeptide fraction (APF) and the IgA fragments, were separated by preparative zonal ultracentrifugation using a sucrose gradient containing 1.5 mM glycodesoxycholate. The purification of the APF was verified by sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis and immunology, and its amino acid composition then was determined. This procedure was used to obtain a polyclonal antiserum directed solely against the APF.

摘要

人类载脂蛋白胆汁脂蛋白复合物(BLC)的两种主要蛋白质成分,即阴离子多肽组分(APF)和IgA片段,通过使用含有1.5 mM甘氨脱氧胆酸盐的蔗糖梯度进行制备性区带超速离心分离。通过十二烷基硫酸钠(SDS)聚丙烯酰胺凝胶电泳和免疫学方法验证了APF的纯化,然后测定了其氨基酸组成。该程序用于获得仅针对APF的多克隆抗血清。

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