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• W2071703000 abstract "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." @default.
• W2071703000 created "2016-06-24" @default.
• W2071703000 creator A5074623028 @default.
• W2071703000 creator A5087909694 @default.
• W2071703000 date "1986-01-01" @default.
• W2071703000 modified "2023-10-16" @default.
• W2071703000 title "Monoclonal antibody affinity purification of a Leishmania membrane glycoprotein and its inhibition of leishmania-macrophage binding." @default.
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• W2071703000 doi "https://doi.org/10.1073/pnas.83.1.100" @default.
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