Regulation of streptokinase-human plasmin complex by the plasma proteinase inhibitors alpha 2-antiplasmin and alpha 2-macroglobulin is species specific and temperature dependent.
Regulation of streptokinase-human plasmin complex by the plasma proteinase inhibitors alpha 2-antiplasmin and alpha 2-macroglobulin is species specific and temperature dependent.
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血浆蛋白酶抑制剂α2-抗纤溶酶和α2-巨球蛋白对链激酶-人纤溶酶复合物的调节具有物种特异性和温度依赖性。
DOI：
10.1182/blood.v72.5.1658.bloodjournal7251658
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发表时间：
1988
期刊：
影响因子：
20.3
通讯作者：
L. L. Braud
中科院分区：
文献类型：
--
作者：
S. Gonias;N. Figler;L. L. Braud
Streptokinase-plasmin complex (SkPl) was prepared with human plasminogen. Regulation of SkPl and plasmin by the plasma proteinase inhibitors, alpha 2-antiplasmin (alpha 2AP) and alpha 2-macroglobulin (alpha 2M), was studied as a function of temperature in plasminogen-depleted human plasma, mouse plasma, and solutions of purified proteins. The reaction of plasmin with proteinase inhibitors in human plasma was complete. alpha 2AP was the predominant inhibitor. The fraction of alpha 2M-plasmin recovered was not affected significantly by incubation temperature. In contrast, the reaction of SkPl with human proteinase inhibitors was markedly temperature dependent. The apparent second-order rate constant for the reaction of SkPl with purified alpha 2AP at 37 degrees C (1.5 x 10(2) mol/L-1 s-1) was greater than 150-fold higher than the constant derived at 4 degrees C. In human plasma and in solutions containing mixtures of purified human proteins, alpha 2AP was the principal inhibitor of SkPl. Elevating the temperature enhanced the reaction of SkPl with alpha 2AP and alpha 2M comparably. Equivalent results were obtained when incubations were performed in platelet-rich plasma (PRP) or whole blood. In murine plasma, SkPl reacted readily with the proteinase inhibitors. The principal inhibitor of SkPl was alpha 2M. Maximum reaction between SkPl and murine alpha 2M was observed at 37 degrees C; however, significant reaction also occurred at 4 degrees C. alpha 2 AP was the predominant inhibitor of plasmin in mouse plasma. Reaction of alpha 2AP with SkPl in murine plasma was significant only after the alpha 2M was inactivated with methylamine. These results were not affected by platelets or whole blood cells. We conclude that the thrombolytic efficacy of streptokinase reflects not only the nature of the plasminogen activator complex but also the function of the proteinase inhibitors.
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人α2-巨球蛋白半分子与纤溶酶的反应作为蛋白酶结合位点结构的探针。
影响因子：
2.9
作者：
Gonias,SL;Pizzo,SV
通讯作者：
Pizzo,SV
α2-巨球蛋白和链激酶-纤溶酶（原）复合物之间的温度依赖性反应。
DOI：
--
发表时间：
1987
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Rajagopalan,S;Gonias,SL;Pizzo,SV
通讯作者：
Pizzo,SV
人、小鼠和大鼠 α-巨球蛋白蛋白酶抑制剂的配体结合、构象变化和血浆消除。
DOI：
10.1042/bj2090099
发表时间：
1983
期刊：
The Biochemical journal
影响因子：
--
作者：
Gonias,SL;Balber,AE;Hubbard,WJ;Pizzo,SV
通讯作者：
Pizzo,SV
DOI：
10.1016/s0021-9258(17)43916-0
发表时间：
1983-12
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
S. Gonias;S. Pizzo
通讯作者：
S. Gonias;S. Pizzo
人纤维蛋白原及其纤溶酶产物增强链激酶催化的人纤溶酶原激活。
影响因子：
2.9
作者：
Strickland,DK;Morris,JP;Castellino,FJ
通讯作者：
Castellino,FJ