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使用单克隆抗体通过免疫亲和层析法分离人髓鞘碱性蛋白。

Isolation of the human myelin basic protein by immunoaffinity chromatography with a monoclonal antibody.

作者信息

Tigyi G J, Balázs L, Monostori E, Andó I

出版信息

Mol Immunol. 1984 Oct;21(10):889-94. doi: 10.1016/0161-5890(84)90144-5.

Abstract

Immunoaffinity chromatography has been developed for the isolation of the human myelin basic protein (MBP). The method is based on the use of a monoclonal antibody which was produced to bovine MBP, cross-reacting with human MBP. The protein isolated from acidic extracts of the brain proteins was shown to be native MBP by its immunochemical reactivity, by its ability to elicit experimental allergic encephalomyelitis and by its mol. wt (18,600 +/- 400). It represented a single-band purity after hypersensitive silver staining. The MBP isolated by the method described represents a higher purity than that of the MBP purified by conventional multistep biochemical separation techniques.

摘要

免疫亲和色谱法已被用于分离人髓鞘碱性蛋白(MBP)。该方法基于使用一种针对牛MBP产生的单克隆抗体,该抗体与人MBP发生交叉反应。从脑蛋白酸性提取物中分离出的蛋白质,通过其免疫化学反应性、引发实验性过敏性脑脊髓炎的能力以及其分子量(18,600±400),被证明是天然MBP。经超敏银染后,它呈现出单带纯度。通过所述方法分离的MBP比通过传统多步生化分离技术纯化的MBP具有更高的纯度。

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