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Namalwa核核糖核蛋白抗原52/5.3的鉴定与纯化。

Identification and purification of Namalwa nuclear RNP antigen 52/5.3.

作者信息

Takahashi K, Chan P K, Busch R K, Busch H

出版信息

J Cancer Res Clin Oncol. 1983;105(1):67-75. doi: 10.1007/BF00391834.

Abstract

Using affinity purified rabbit antibodies to HeLa nucleoli and the Western blotting techniques, an antigen with an approximate molecular weight of 52,000 and pI of 5.3 was found in Namalwa cells (a Burkitt lymphoma), but not in normal liver cells. This antigen was purified from Namalwa RNP by column chromatography on Sephacryl S-200, hydroxylapatite and one-dimensional SDS gel electrophoresis. A liver protein with the same molecular weight and pI value was purified from RNP fraction by one-dimensional SDS gel electrophoresis. Both proteins had similar amino-acid compositions. The tryptic map of 125I-labeled protein 52/5.3 contained approximately nine major spots; spot 9 was present in the Namalwa protein but not in the liver protein. The similarity of the structures of these proteins and their differences in antigenicity are noteworthy and require further structural and functional analysis.

摘要

利用亲和纯化的兔抗HeLa核仁抗体及蛋白质免疫印迹技术,在Namalwa细胞(一种伯基特淋巴瘤细胞)中发现了一种分子量约为52,000且等电点为5.3的抗原,而在正常肝细胞中未发现。该抗原通过Sephacryl S - 200柱层析、羟基磷灰石柱层析及一维SDS凝胶电泳从Namalwa核糖核蛋白中纯化得到。通过一维SDS凝胶电泳从核糖核蛋白组分中纯化出一种分子量和等电点值相同的肝脏蛋白。两种蛋白质具有相似的氨基酸组成,但125I标记的52/5.3蛋白的胰蛋白酶图谱包含约9个主要斑点,其中斑点9存在于Namalwa蛋白中而不存在于肝脏蛋白中。这些蛋白质结构的相似性及其抗原性的差异值得关注,需要进一步进行结构和功能分析。

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