Wiman B
Eur J Biochem. 1977 Jun 1;76(1):129-37. doi: 10.1111/j.1432-1033.1977.tb11578.x.
The primary structure of the human plasmin B-chain has been determined. It consists of 230 residues divided in three cyanogen bromide fragments: The amino-terminal 24 residues, the carboxy-terminal three residues and the middle 203 residues. Sequence detemination was performed on the tryptic and the chymotryptic peptides obtained from the main cyanogen bromide fragment of this chain. Owing to similarities between some of the overlapping chymotryptic peptides, two different sequences were possible from these results. However, since the homologies with the pancreatic serine proteases and also the B-chains of thrombin and factor XA are pronounced, the arrangement still could be settled. By peptic digestion of partially reduced and S-carboxymethylated B-chain it was shown that there are two interchain disulphide bridges, which connect the A and B-chains of plasmin, involving Cys-5 and Cys-105 from the B-chain. The intrachain disulphides in the B-chain seem to be situated exactly as in chymotrypsin as partly judged from homologies.
人纤溶酶B链的一级结构已被确定。它由230个残基组成，分为三个溴化氰片段：氨基末端的24个残基、羧基末端的三个残基和中间的203个残基。对从该链的主要溴化氰片段获得的胰蛋白酶肽和糜蛋白酶肽进行了序列测定。由于一些重叠的糜蛋白酶肽之间存在相似性，根据这些结果可能有两种不同的序列。然而，由于与胰腺丝氨酸蛋白酶以及凝血酶和因子XA的B链有明显的同源性，其排列方式仍可确定。通过对部分还原和S-羧甲基化的B链进行胃蛋白酶消化，结果表明有两个链间二硫键，它们连接纤溶酶的A链和B链，涉及B链中的Cys-5和Cys-105。从同源性部分判断，B链中的链内二硫键似乎与胰凝乳蛋白酶中的位置完全相同。
