Bhowal J, Mitra A, Banerjee S, Sikdar S, Guha A K, Chatterjee B P
Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata 700 032, India.
Indian J Biochem Biophys. 2004 Apr-Jun;41(2-3):81-8.
An agglutinin, a monomeric glycoprotein with a molecular mass of about 6.5 kDa and containing 18% sugar has been purified to an apparent homogeneity from a 21 days old culture filtrate of an anthropophilic dermatophyte Tricophyton rubrum. It is a human blood group non-specific agglutinin which also agglutinates animal erythrocytes and Ehrlich ascites carcinoma and Sarcoma-180 cells. It is thermally stable and exhibits maximum activity at pH 8. Amino acid analysis shows a significant amount of glycine, with no cysteine. Glycoproteins inhibited the hemagglutination of the agglutinin, but not the simple sugars, including sialic acid. Fetuin is the most potent inhibitor among the glycoproteins tested. This inhibition gives a hint to binding with Galbeta1-3GalNAc or Galbeta1-4GlcNAc residue containing sialic acid at the terminal position with alpha 2-6 or alpha 2-3 linkage.
一种凝集素已从亲人性皮肤癣菌红色毛癣菌21日龄的培养滤液中纯化至表观均一状态，它是一种单体糖蛋白，分子量约为6.5 kDa，含糖量为18%。它是一种人血型非特异性凝集素，也能凝集动物红细胞、艾氏腹水癌细胞和肉瘤180细胞。它具有热稳定性，在pH 8时表现出最大活性。氨基酸分析显示含有大量甘氨酸，无半胱氨酸。糖蛋白可抑制该凝集素的血凝作用，但包括唾液酸在内的单糖则无此作用。在所测试的糖蛋白中，胎球蛋白是最有效的抑制剂。这种抑制作用提示其与末端含有唾液酸且通过α2-6或α2-3连接的Galβ1-3GalNAc或Galβ1-4GlcNAc残基结合。
