Budzynski A Z, Marder V J
Thromb Haemost. 1977 Dec 15;38(4):793-800.
The molecular weights of derivatives obtained from chemical and enzymatic degradation of fibrinogen and fibrin support a model in which the two halves of the fibrinogen molecule are covalently linked by a set of disulfide bonds at the amino-terminal region. The 2 asymmetric cleavages caused by plasmin in the fibrinogen molecule occur according to the reactions: X leads to Y + D Y leads to E + D. The quantitative analysis of the amino-terminal amino acids in fragments D (from fibrinogen) and DD (from crosslinked fibrin) yields a total of 3.0 and 6.9 moles of amino acids per mole of protein, indicating three and six polypeptide chain structures, respectively. The data on molecular weights, polypeptide chain composition and immunologic properties of fibrinogen degradation products support the hypothesis on the asymmetric pathway of fibrinogen degradation by plasmin and the formation of two fragment D and one fragment E molecules from each molecule of fibrinogen.
从纤维蛋白原和纤维蛋白的化学及酶促降解获得的衍生物的分子量支持这样一种模型，即纤维蛋白原分子的两半在氨基末端区域通过一组二硫键共价连接。纤溶酶在纤维蛋白原分子中引起的2次不对称裂解按照以下反应发生：X生成Y + D，Y生成E + D。对片段D（来自纤维蛋白原）和DD（来自交联纤维蛋白）中氨基末端氨基酸的定量分析得出，每摩尔蛋白质分别有3.0和6.9摩尔氨基酸，分别表明有三条和六条多肽链结构。关于纤维蛋白原降解产物的分子量、多肽链组成和免疫特性的数据支持关于纤溶酶对纤维蛋白原的不对称降解途径以及每个纤维蛋白原分子形成两个片段D和一个片段E分子的假说。
