Watt K W, Takagi T, Doolittle R F
Biochemistry. 1979 Jan 9;18(1):68-76. doi: 10.1021/bi00568a011.
The beta chain of human fibrinogen contains 461 amino acid residues, 15 of which are methionines. The calculated molecular weight, independent of a single carbohydrate cluster, is 52 230. In this regard, we have isolated and characterized all 16 cyanogen bromide fragments. In one case (CNI), we have concentrated on a disputed portion of a previously reported fragment. The arrangement of the cyanogen bromide peptides was deduced by the use of overlap fragments obtained from the tryptic digestion of modified and unmodified beta-chains and from digestions with staphylococcal protease, as well as by considerations involving the plasmic digestion products of fibrinogen. In one case two adjacent fragments were aligned by homology with the corresponding segments of the gamma chain. The homology of the beta chain with the gamma chain is especially strong over the course of the carboxy-terminal two-thirds of the sequence. Neither of these chains appears to be homologous with the alpha chain in these regions. With a few minor exceptions, the sequence reported in this article is in agreement with data reported by other groups in Stockholm and Munich.
人纤维蛋白原的β链含有461个氨基酸残基，其中15个是甲硫氨酸。不考虑单个碳水化合物簇时，计算出的分子量为52230。在这方面，我们已经分离并鉴定了所有16个溴化氰片段。在一个案例（CNI）中，我们专注于先前报道片段中一个有争议的部分。溴化氰肽段的排列是通过使用从修饰和未修饰的β链的胰蛋白酶消化以及葡萄球菌蛋白酶消化中获得的重叠片段推导出来的，同时也考虑了纤维蛋白原的纤溶酶消化产物。在一个案例中，两个相邻片段通过与γ链的相应片段的同源性进行了比对。β链与γ链在序列羧基末端三分之二的过程中同源性特别强。在这些区域中，这两条链似乎都与α链没有同源性。除了一些小的例外，本文报道的序列与斯德哥尔摩和慕尼黑的其他研究小组报道的数据一致。
