微纤溶酶的结构与形成
Structure and formation of microplasmin.
作者信息
Wu H L, Shi G Y, Wohl R C, Bender M L
机构信息
Biochemistry Department, Medical College, National Cheng-Kung University, Taiwan, Republic of China.
出版信息
Proc Natl Acad Sci U S A. 1987 Dec;84(24):8793-5. doi: 10.1073/pnas.84.24.8793.
The structure of human microplasmin, prepared from plasmin in alkaline solution, has been studied. Microplasmin consists of two polypeptide chains connected by disulfide bonds. One polypeptide is the B chain of plasmin consisting of 230 amino acids, and the other peptide is the COOH-terminal portion of the A chain of plasmin consisting of 31 amino acid residues. Microplasmin has a molecular weight of 28,635, calculated from its primary sequence. It is slightly more positively charged than plasminogen and is a more hydrophobic molecule. The proposed scheme for the formation of microplasmin involves autolysis at specific peptide bonds and scrambling of especially sensitive disulfide bonds in alkaline solution.
对在碱性溶液中由纤溶酶制备的人微纤溶酶的结构进行了研究。微纤溶酶由通过二硫键连接的两条多肽链组成。一条多肽是由230个氨基酸组成的纤溶酶B链，另一条肽是由31个氨基酸残基组成的纤溶酶A链的COOH末端部分。根据其一级序列计算，微纤溶酶的分子量为28,635。它的正电荷比纤溶酶原略多，是一个疏水性更强的分子。提出的微纤溶酶形成方案涉及在碱性溶液中特定肽键的自溶和特别敏感的二硫键的重排。
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