期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1986
卷号：83
期号：1
页码：100-104
DOI：10.1073/pnas.83.1.100
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Specific monoclonal antibody coupled to Affi-Gel 10 was used to purify a major membrane glycoprotein of Leishmania mexicana amazonensis, one of a group of parasitic protozoa that specifically infect mammalian macrophages. Immobilized antigen was eluted at a 34% efficiency with buffers at either pH 2.5 or 11 or with MgCl2, but only the antigen eluted under basic conditions could be readsorbed to the immunobeads. Sephacryl S-300 gel filtration of the purified antigen gave a single peak of protein estimated to have a molecular mass of 400 kDa. However, NaDodSO4/polyacrylamide gel electrophoresis showed a single band of this protein with an apparent molecular mass of 63 kDa. The antigen is an N-linked glycoprotein, as indicated by its increase in electrophoretic mobility after treatment with endoglycosidase H and by its binding to lentil lectin-Sepharose, elutable with methyl alpha-D-mannoside and methyl alpha-D-glucoside. Purified antigen inhibits the binding of leishmania cells to macrophages by 50%, suggesting that it may play a role in the process of infection.
