Harth G, Haidaris C G, So M
Department of Molecular Biology, Scripps Clinic and Research Foundation, La Jolla, CA.
Mol Biochem Parasitol. 1989 Mar 1;33(2):143-50. doi: 10.1016/0166-6851(89)90028-5.
Four developmentally regulated glycoproteins were purified from detergent solubilized cell membranes of Trypanosoma cruzi. Three trypomastigote specific glycoproteins each migrated as single bands under denaturing conditions with approximate Mr of 90,000, 85,000, and 55,000 and pI values of 4.3-5.0, 8.5-9.1, and 8.2, respectively. The fourth, epimastigote specific, protein had an approximate Mr of 72,000 and a pI of 4.8-5.1. The Mr of all four glycoproteins changed by 5-50% upon endoglycosidase F treatment. The Mr 72,000 antigen was the only one that reacted strongly with anti-epimastigote sera raised in rabbits. Sera from a Chagasic patient reacted strongly with the three trypomastigote specific glycoproteins and very weakly with the Mr 72,000 glycoprotein.
从克氏锥虫去污剂溶解的细胞膜中纯化出四种受发育调控的糖蛋白。三种锥鞭毛体特异性糖蛋白在变性条件下均迁移为单一条带，其近似分子量分别为90,000、85,000和55,000，pI值分别为4.3 - 5.0、8.5 - 9.1和8.2。第四种，即前鞭毛体特异性蛋白，其近似分子量为72,000，pI为4.8 - 5.1。用内切糖苷酶F处理后，所有四种糖蛋白的分子量变化了5% - 50%。分子量为72,000的抗原是唯一与兔体内产生的抗前鞭毛体血清强烈反应的抗原。恰加斯病患者的血清与三种锥鞭毛体特异性糖蛋白强烈反应，而与分子量为72,000的糖蛋白反应非常微弱。
