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木瓜蛋白酶溶解的TL抗原的亚片段。

Subfragments of the papain solubilized TL antigen.

作者信息

Stanton T H, Bennett J C, Wolcott M

出版信息

J Immunol. 1975 Oct;115(4):1013-7.

PMID:1176764
Abstract

TL antigen was solubilized from the tumor ASLI (TL. 1,2,3) by papain digestion. The subfragments of 125I-labeled TL were examined by two methods. The first involved immune precipitation followed by electrophoresis on SDS-acrylamide gels. This treatment yielded three bands of molecular weight 39,000 and 19,000, as well as material which migrated with the tracking dye. In the second procedure the papain digested material was partially purified on Sephadex G-200. The active fraction from G-200 was labeled with 125Iodine, mixed with alloantiserum and rechromatographed on G-200. The isolated immune complexes were boiled in SDS and 2-mercaptoethanol, then separated on a SDS-Sephadex G-150 column. Two radioactive peaks were eluted indicating an absence of the 19,000 m.w. component following the latter method of purification.

摘要

通过木瓜蛋白酶消化从肿瘤ASLI(TL. 1,2,3)中溶解出TL抗原。用两种方法检测了125I标记的TL的亚片段。第一种方法是免疫沉淀,然后在SDS-丙烯酰胺凝胶上进行电泳。这种处理产生了分子量为39,000和19,000的三条带,以及与示踪染料一起迁移的物质。在第二种方法中,将木瓜蛋白酶消化的物质在Sephadex G-200上进行部分纯化。来自G-200的活性部分用125碘标记,与同种抗血清混合并在G-200上重新层析。分离出的免疫复合物在SDS和2-巯基乙醇中煮沸,然后在SDS-Sephadex G-150柱上分离。洗脱了两个放射性峰,表明采用后一种纯化方法后不存在分子量为19,000的成分。

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