参与牛III型胶原分子间交联的溴化氰肽段的鉴定
Identification of cyanogen bromide peptides involved in intermolecular cross-linking of bovine type III collagen.
作者信息
Nicholls A C, Bailey A J
出版信息
Biochem J. 1980 Jan 1;185(1):195-201. doi: 10.1042/bj1850195.
Abstract
Cyanogn 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.
摘要
从牛III型胶原蛋白中分离并鉴定出含有可还原交联键的溴化氰肽。分子螺旋部分的两种肽，α1(III)CB7和α1(III)CB9B，显示在形成交联键时含有与非螺旋“醛供体”残基交联的“氨基供体”残基。该信息与先前发表的关于溴化氰肽顺序的数据[菲茨克、奥尔曼、劳特伯格和瓦赫特(1977年)《美国国家科学院院刊》74, 84 - 86]相结合，表明在III型胶原蛋白中，分子间交联位于末端重叠区域，从而以与I型和II型胶原蛋白类似的方式稳定纤维内分子的四分之一交错排列。
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