Sawada J I, Shioiri-Nakano K, Osawa T
Transplantation. 1975 Apr;19(4):335-42. doi: 10.1097/00007890-197504000-00009.
Guinea pig lymphotoxin (LT) produced by stimulation of lymph node cells with Phaseolus vulgaris phytohemagglutinin was purified approximately 1,000-fold in specific activity by ammonium sulfate fractionation, DEAE-Sephadex column chromatography, and gel filtration on Sephadex G-100. The properties of LT tested at the various stages of purification revealed that the LT was a heat-sensitive, protease-sensitive proteinaceous substance, and its approximate molecular weight was estimated to be 50,000 by means of gel filtration. The most purified fraction (Fr. D) was found to be devoid of the activities of migration inhibitory and mitogenic factors, clearly indicating that these activities are mediated by different substances.
用菜豆植物血凝素刺激淋巴结细胞产生的豚鼠淋巴毒素（LT），通过硫酸铵分级分离、DEAE-葡聚糖凝胶柱色谱和葡聚糖凝胶G-100凝胶过滤，比活性纯化了约1000倍。在纯化的各个阶段测试的LT特性表明，LT是一种对热敏感、对蛋白酶敏感的蛋白质物质，通过凝胶过滤估计其近似分子量为50,000。发现最纯的级分（级分D）没有迁移抑制因子和促有丝分裂因子的活性，清楚地表明这些活性是由不同物质介导的。
