Andrianov S I, Makogonenko E M, Kudinov S A
Ukr Biokhim Zh (1978). 1992 Mar-Apr;64(2):31-8.
A comparative analysis of the rates of polymeric fibrin structure destruction by plasmin (Pm) and its proteolytic derivatives such as Val354-plasmin (c-Pm), Val442-plasmin (m-Pm) and Lys530-plasmin (mu-Pm) has been undertaken. It was shown, that Pm, c-Pm, m-Pm and mu-Pm at equal proteolytic activity, have dissolved fibrin clots with relative rates 40.3:38.0:4.6:1.0 correspondingly. The Pm, m-Pm and mu-Pm relative rates were changed by epsilon-aminocaproic acid to 4.6:1.5:1.0 correspondingly. In this case fibrin clot destruction time was increased for Pm and m-Pm and was not changed for mu-Pm. The rates of fibrinogen hydrolysis were nearly equal for these forms of enzyme. It was suggested, that the specific interactions between plasmin K4 and K5 kringles and solid phase fibrin substrate determine the polymer fibrin structure destruction rate.
已对纤溶酶（Pm）及其蛋白水解衍生物如Val354 - 纤溶酶（c - Pm）、Val442 - 纤溶酶（m - Pm）和Lys530 - 纤溶酶（μ - Pm）对聚合纤维蛋白结构的破坏速率进行了比较分析。结果表明，在蛋白水解活性相等的情况下，Pm、c - Pm、m - Pm和μ - Pm溶解纤维蛋白凝块的相对速率分别为40.3:38.0:4.6:1.0。ε - 氨基己酸使Pm、m - Pm和μ - Pm的相对速率分别变为4.6:1.5:1.0。在这种情况下，Pm和m - Pm的纤维蛋白凝块破坏时间增加，而μ - Pm的则未改变。这些酶形式对纤维蛋白原的水解速率几乎相等。有人提出，纤溶酶K4和K5kringle与固相纤维蛋白底物之间的特异性相互作用决定了聚合纤维蛋白结构的破坏速率。
