[Isolation and purification of a membrane hyaluronate-binding protein from embryonic human brain].

V L Tkach, G A Ushakova, E A Lepekhin
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Abstract

A membrane hyaluronate-binding protein from cerebral cortex of human embryonic brain (22-24 weeks) was purified by affinity, ion exchange chromatographies and gel-filtration. While gel-filtration analysis the protein had Mm 250 kDa. Electrophoresis under reduction conditions in the presence of DS-Na revealed a major band with Mm 85 kDa and two minor binds with Mm 68 and 36 kDa. The isolated protein did not react with antibodies against known hyaluronate-binding and other proteins with similar mass. The results show that a new membrane hyaluronate-binding protein was isolated and purified from human embryonic brain.

[从胚胎人脑中分离纯化透明质酸膜结合蛋白]。
采用亲和层析、离子交换层析和凝胶过滤等方法纯化了22-24周人胚胎大脑皮层透明质酸膜结合蛋白。凝胶过滤分析蛋白的Mm为250 kDa。在DS-Na存在的还原条件下,电泳显示一个主要带与Mm 85 kDa结合,两个次要带与Mm 68和36 kDa结合。分离的蛋白不与已知的透明质酸结合蛋白和其他类似质量蛋白的抗体发生反应。结果表明,从人胚胎脑中分离纯化了一种新的透明质酸膜结合蛋白。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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