Irsigler K, Lechner K, Deutsch E
First Medical Department, University of Vienna.
Thromb Diath Haemorrh. 1965 Sep 1;14(1-2):18-31.
Purified brain tissue thromboplastins of human, bovine and chicken origin have been tested on homologous and heterologous plasmas. Purified brain tissue thromboplastin is species specific. Lipid extracts from purified brain tissue thromboplastin prepared with pyridin show a negligable residual species specificity, probably caused by a slight contamination with brain tissue thromboplastin. The activity curves of our lipid extracts differ from typical curves expected for lipid activators by a less distinct inhibition in high concentrations probably caused by a different composition of petrol-ether and pyridin extracts. The protein part of tissue thromboplastin does not activate prothrombin in any system. The protein part of tissue thromboplastin of one species could be combined with the lipid part of another species to form an active tissue thromboplastin. The species specificity of these combinations was determined by the source of protein used.
已对源自人、牛和鸡的纯化脑组织凝血活酶在同源和异源血浆上进行了测试。纯化脑组织凝血活酶具有物种特异性。用吡啶制备的纯化脑组织凝血活酶的脂质提取物显示出可忽略不计的残留物种特异性,这可能是由于轻微污染了脑组织凝血活酶所致。我们的脂质提取物的活性曲线与脂质激活剂预期的典型曲线不同,在高浓度下抑制作用不太明显,这可能是由于石油醚提取物和吡啶提取物的组成不同所致。组织凝血活酶的蛋白质部分在任何系统中均不激活凝血酶原。一个物种的组织凝血活酶的蛋白质部分可与另一个物种的脂质部分结合形成活性组织凝血活酶。这些组合的物种特异性由所用蛋白质的来源决定。