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Identification of cyanogen bromide peptides involved in intermolecular cross-linking of bovine type III collagen

机译:鉴定与牛III型胶原分子间交联的溴化氰肽

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pCyanogn bromide peptides derived from bovine type III collagen and containing reducible cross-links were isolated and identified. Two peptides, alpha 1 (III)CB7 and alpha 1 (III)CB9B, from within the helical portion of the molecule were shown to contain the ‘amino donor’ residues cross-linked to non-helical ‘aldehyde donor’ residues in the formation of cross-links. This information, in conjunction with previously published data for the order of the cyanogen bromide peptides [Fietzek, Allman, Rauterberg & Wachter (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 84-86], suggests that in type III collagen intermolecular cross-links are located in the end-overlap regions, so as to stabilize a quarter-stagger arrangement of molecules within the fibre in a similar manner to that proposed for type I and type II collagens./p
机译:分离并鉴定了来源于牛III型胶原并含有可还原交联的Cyanogn溴化物肽。分子螺旋部分中的两个肽,即α1(III)CB7和α1(III)CB9B被显示含有与地层中非螺旋“醛供体”残基交联的“氨基供体”残基交叉链接。该信息与先前公布的溴化氰肽顺序有关的数据[Fietzek,Allman,Rauterberg& A. Wachter(1977)Proc。 Natl。学院科学USA 74,84-86],建议在III型胶原中,分子间交联位于末端重叠区域,以便以与针对类型提议的相似的方式稳定纤维内分子的四分之一交错排列I型和II型胶原蛋白。

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