Joist J H, Niewiarowski S, Nath N, Mustard J F
J Lab Clin Med. 1976 Apr;87(4):659-69.
Antiplasmin activity was shown to be released from washed pig platelets by thrombin following a time course similar to that of 3H-serotonin. Antiheparin activity (platelet factor 4) appeared to be released by thrombin at a slower rate than 3H-serotonin or antiplasmin activity. Subcellular fractionation of pig platelets showed that the storage site for antiplasmin is probably the dense (amine storage) granules. Antiheparin was distributed among all of the subcellular particulate fractions except the fraction rich in dense granules. Material released from washed pig platelets and concentrated by ZnSO4 precipitation (crude antiheparin) was found to be rich in antiplasmin activity. Gel filtration on Sephadex G-150, DEAE cellulose column chromatography, and polyacrylamide gel electrophoresis showed that pig platelet antiplasmin is a low molecular weight (approximately 30,000 d) material of alpha1-globulin electrophoretic mobility. It was found to be heat labile and also inhibitory to the caseinolytic activity of trypsin but had no effect on the action of thrombin on fibrinogen. These data indicate that platelet antiplasmin is distinct from platelet antiheparin.
抗纤溶酶活性经凝血酶作用后从洗涤过的猪血小板中释放出来，其时间进程与3H-5-羟色胺相似。抗肝素活性（血小板第4因子）似乎比3H-5-羟色胺或抗纤溶酶活性释放得慢。猪血小板的亚细胞分级分离表明，抗纤溶酶的储存部位可能是致密（胺储存）颗粒。抗肝素分布于除富含致密颗粒的部分之外的所有亚细胞颗粒部分。从洗涤过的猪血小板中释放并经硫酸锌沉淀浓缩的物质（粗制抗肝素）富含抗纤溶酶活性。在葡聚糖凝胶G-150上进行凝胶过滤、DEAE纤维素柱层析和聚丙烯酰胺凝胶电泳表明，猪血小板抗纤溶酶是一种电泳迁移率为α1球蛋白的低分子量（约30,000道尔顿）物质。发现它对热不稳定，并且对胰蛋白酶的酪蛋白水解活性有抑制作用，但对凝血酶作用于纤维蛋白原没有影响。这些数据表明血小板抗纤溶酶与血小板抗肝素不同。
