纤溶酶原激活切割位点的氨基酸序列：与凝血酶原“原”部分的同源性。
Amino-acid sequence of activation cleavage site in plasminogen: homology with "pro" part of prothrombin.
作者信息
Sottrup-Jensen L, Zajdel M, Claeys H, Petersen T E, Magnusson S
出版信息
Proc Natl Acad Sci U S A. 1975 Jul;72(7):2577-81. doi: 10.1073/pnas.72.7.2577.
A 38-residue fragment is isolated from carboxymethylated plasminogen. Residues 29-38 have the same sequence as the amino-terminal end of the light chain of plasmin. The sequence 1-28 is therefore the sequence of the carboxyl-terminal end of the heavy chain and contains the specific sequence at which urokinase (EC 3.4.99.26) and other plasminogen-activating serine proteases split. Two of the five carboxymethyl-cysteine residues in the isolated fragment are situated close to the cleavage site and the fragment is not itself a substrate for plasminogen-activators. Residues 1-11 show extensive sequence homology with residues 137-147 and 242-252 in prothrombin, which are located in corresponding regions of the two internally homologous 83-residue structures in the non-thrombin part of the molecule, indicating that such structures may be a common feature of the non-protease part of the larger serine protease zymogens.
从羧甲基化纤溶酶原中分离出一个38个残基的片段。第29 - 38位残基与纤溶酶轻链的氨基末端序列相同。因此，第1 - 28位序列是重链羧基末端的序列，并且包含尿激酶（EC 3.4.99.26）和其他纤溶酶原激活丝氨酸蛋白酶切割的特定序列。分离片段中的五个羧甲基半胱氨酸残基中有两个位于切割位点附近，并且该片段本身不是纤溶酶原激活剂的底物。第1 - 11位残基与凝血酶原中的第137 - 147位和242 - 252位残基显示出广泛的序列同源性，它们位于分子非凝血酶部分的两个内部同源83个残基结构的相应区域，表明这种结构可能是较大丝氨酸蛋白酶原非蛋白酶部分的共同特征。
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