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通过结构域特异性抗体结合有限蛋白酶解和S-氰化作用揭示的细胞周围基质纤连蛋白和血浆纤连蛋白之间的结构域差异:初步报告

Differences in domain structure between pericellular matrix and plasma fibronectins as revealed by domain-specific antibodies combined with limited proteolysis and S-cyanylation: a preliminary note.

作者信息

Sekiguchi K, Siri A, Zardi L, Hakomori S

出版信息

Biochem Biophys Res Commun. 1983 Oct 31;116(2):534-40. doi: 10.1016/0006-291x(83)90556-9.

Abstract

Differences in domain structure between human fibronectins obtained from pericellular matrix and plasma have been revealed by limited proteolysis and S-cyanylation, followed by identification of each domain with domain-specific antibodies. Although the overall domain structure is similar between pericellular and plasma fibronectins, the fragments derived from the COOH-terminal region of these fibronectins, which were defined by specific antibodies, exhibited clear differences in their molecular weights and protease susceptibility, suggesting that the structure near the COOH-terminal region is significantly different between these two proteins.

摘要

通过有限蛋白酶解和S-氰化作用,随后用结构域特异性抗体鉴定各个结构域,已揭示了从细胞周围基质和血浆中获得的人纤连蛋白在结构域结构上的差异。尽管细胞周围纤连蛋白和血浆纤连蛋白的整体结构域结构相似,但由特异性抗体定义的源自这些纤连蛋白COOH末端区域的片段,在分子量和蛋白酶敏感性方面表现出明显差异,这表明这两种蛋白质在COOH末端区域附近的结构存在显著差异。

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