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冷球蛋白IgM-κ McE的Fab μ和(Fc)5 μ片段的拉曼光谱及构象结构

Raman spectra and conformational structures of Fab mu and (Fc)5 mu fragments of cryoglobulin IgM-kappa McE.

作者信息

Thomas G J, Prescott B, Middaugh C R, Litman G W

出版信息

Biochim Biophys Acta. 1979 Apr 25;577(2):285-90. doi: 10.1016/0005-2795(79)90032-1.

Abstract

Raman spectra have been obtained on aqueous solutions of the following human immunoglobulins: IgM-kappa McE, IgG-kappa Ger, IgM-kappa WSm and IgG-lambda Gui. The former two species exhibit the property of cryoprecipitation. Comparison of the spectra shows that all immunoglobulins have similar secondary structures, predominantly of the beta-sheet type. Fab mu and (Fc)5 mu fragments of IgM-kappa McE also yield Raman spectra which indicate closely similar secondary structures. Minor differences among the spectra can be explained by differences in amino acid compositions of the respective proteins.

摘要

已获得以下人类免疫球蛋白水溶液的拉曼光谱

IgM-κMcE、IgG-κGer、IgM-κWSm和IgG-λGui。前两种物质具有冷沉淀特性。光谱比较表明,所有免疫球蛋白都具有相似的二级结构,主要为β-折叠类型。IgM-κMcE的Fab μ和(Fc)5 μ片段也产生拉曼光谱,表明其二级结构非常相似。光谱之间的微小差异可以用各蛋白质氨基酸组成的差异来解释。

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