Timpl R, Fietzek P P, van Delden V, Landrath G
Hoppe Seylers Z Physiol Chem. 1978 Nov;359(11):1553-60. doi: 10.1515/bchm2.1978.359.2.1553.
Three disulfide-linked peptides with molecular weights of about 6000, 7000 and 45000, respectively, were isolated from bovine fibrinogen cleaved with cyanogen bromide. The chain constituents of these peptides were separated after reduction and alkylation and identified by partial amino acid sequence analysis. Of the five polypeptide chains of the largest fragment F-CB2, three are derived from the central region of Bbeta chain, one from the Aalpha chain and one from the gamma chain. The smaller peptides F-CB4 and F-CB5 consist of one and two polypeptide chains and originate from central regions of the Bbeta and gamma chains, respectively, indicating that they represent intrachain disulfide loops. These and previous data show that the disulfide-bonded regions of bovine fibrinogen are similar to those in human fibrinogen.
从用溴化氰裂解的牛纤维蛋白原中分离出三种分别具有约6000、7000和45000分子量的二硫键连接的肽。这些肽的链成分在还原和烷基化后被分离，并通过部分氨基酸序列分析进行鉴定。在最大片段F-CB2的五条多肽链中，三条来自Bβ链的中央区域，一条来自Aα链，一条来自γ链。较小的肽F-CB4和F-CB5分别由一条和两条多肽链组成，分别起源于Bβ链和γ链的中央区域，表明它们代表链内二硫键环。这些数据和以前的数据表明，牛纤维蛋白原的二硫键结合区域与人类纤维蛋白原中的相似。
