Han C H, Liu Q H, Ng T B, Wang H X
State Key Laboratory for Agrobiotechnology, Department of Microbiology, China Agricultural University, Beijing, 100094, China.
Biochem Biophys Res Commun. 2005 Oct 14;336(1):252-7. doi: 10.1016/j.bbrc.2005.08.068.
A homodimeric lactose-binding lectin with a molecular mass of 64kDa was isolated from fresh fruiting bodies of the split gill mushroom Schizophyllum commune. The N-terminal sequence of the lectin is similar to a part of the sequence of the cell division protein from Gleobacter violaceus. The lectin was isolated by using a procedure which involved ion exchange chromatography on DEAE-cellulose, CM-cellulose, and Q-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The hemagglutinating activity of the lectin was stable at temperatures up to 40 degrees C, and in concentrations of NaOH and HCl solution up to 125 and 25mM, respectively. The lectin exhibited potent mitogenic activity toward mouse splenocytes, antiproliferative activity toward tumor cell lines, and inhibitory activity toward HIV-1 reverse transcriptase. It was devoid of antifungal activity.
从裂褶菌新鲜子实体中分离出一种分子量为64kDa的同型二聚体乳糖结合凝集素。该凝集素的N端序列与紫色杆菌属细胞分裂蛋白序列的一部分相似。通过在DEAE-纤维素、CM-纤维素和Q-琼脂糖上进行离子交换色谱，以及在Superdex 75上通过快速蛋白质液相色谱进行凝胶过滤的方法分离该凝集素。该凝集素的血凝活性在高达40℃的温度下稳定，在NaOH和HCl溶液浓度分别高达125mM和25mM时也稳定。该凝集素对小鼠脾细胞表现出强大的促有丝分裂活性，对肿瘤细胞系具有抗增殖活性，对HIV-1逆转录酶具有抑制活性。它没有抗真菌活性。
