Wang H X, Ng T B, Liu W K, Ooi V E, Chang S T
Department of Biology, Chinese University of Hong Kong, New Territories, Hong Kong.
Int J Pept Protein Res. 1995 Dec;46(6):508-13. doi: 10.1111/j.1399-3011.1995.tb01606.x.
Two lectins, TML-1 and TML-2, were isolated from Tricholoma mongolicum by ion-exchange chromatography and gel filtration. They are dimers with molecular weight near 37000. The hemagglutinating activities of TML-1 and TML-2 are sensitive to lactose inhibition and are stable between 10 and 80 degrees C. They exhibit antiproliferative activities against mouse monocyte-macrophage PU5-1.8 cells and mouse mastocytoma P815 cells in vitro. The two lectins differ in the content of proline and tyrosine residues. Both are non-glycoproteins and have hydroxyproline residues.
通过离子交换色谱法和凝胶过滤从蒙古口蘑中分离出两种凝集素,即TML-1和TML-2。它们是分子量接近37000的二聚体。TML-1和TML-2的血凝活性对乳糖抑制敏感,在10至80摄氏度之间稳定。它们在体外对小鼠单核巨噬细胞PU5-1.8细胞和小鼠肥大细胞瘤P815细胞具有抗增殖活性。这两种凝集素在脯氨酸和酪氨酸残基的含量上有所不同。两者均为非糖蛋白且含有羟脯氨酸残基。