Wiman B, Wallén P
Eur J Biochem. 1975 Oct 15;58(2):539-47. doi: 10.1111/j.1432-1033.1975.tb02403.x.
The complete amino acid sequence of a cyanogen bromide fragment (122 residues) obtained from plasminogen is described. This fragment forms the overlap between heavy (A) and light (B) chains of human plasmin. The particular arginyl-valyl bond cleaved in the second step of the activation process is shown to be Arg98-Val99 in this fragment. This site is not very similar to the one in the NH2-terminal part of the molecule (Arg68-Met69). Remarkable homologies with the 'triple loops' ('kringle structures') found in the non-thrombin part of prothrombin are demonstrated. Homologies occurred during evolution of this chain.
本文描述了从纤溶酶原获得的一个溴化氰片段（122个残基）的完整氨基酸序列。该片段构成了人纤溶酶重链（A）和轻链（B）之间的重叠部分。在激活过程第二步中被切割的特定精氨酰-缬氨酰键在该片段中显示为Arg98-Val99。此位点与分子氨基末端部分的位点（Arg68-Met69）不太相似。在凝血酶原非凝血酶部分发现的“三环”（“kringle结构”）显示出显著的同源性。这种同源性在该链的进化过程中出现。
