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- W2009193781 abstract "We partially purified the human immunodeficiency virus (HIV) glycoprotein gp41 from infected H9 cells by immunoaffinity chromatography using a column containing the M25 monoclonal antibody (diMarzo-Veronese et al., 1985). A pH 11.5 buffer worked best for eluting the glycoprotein from this column. The eluted gp41 was used in a sensitive slot blot immunoassay to detect antibodies to HIV in human sera and to prepare rabbit polyclonal antibodies and the 41-1S mouse monoclonal antibody. These antibodies reacted with gp41 in immunoprecipitation and in Western blot assays, but did not neutralize HIV in a syncytiumforming microassay. A pH 2.5 buffer was found to be the most effective solution for eluting gp41 from a 41-1S monoclonal antibody column." @default.
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- W2009193781 date "1988-01-01" @default.
- W2009193781 modified "2023-09-26" @default.
- W2009193781 title "Partial Purification of Native HIV Transmembrane Protein gp41: Generation of Polyclonal and Monoclonal Antibodies" @default.
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- W2009193781 doi "https://doi.org/10.1089/aid.1988.4.51" @default.
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