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pubmed-article:3259140pubmed:abstractTextWe 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 syncytium-forming microassay. A pH 2.5 buffer was found to be the most effective solution for eluting gp41 from a 41-1S monoclonal antibody column.lld:pubmed
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pubmed-article:3259140pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:3259140pubmed:articleTitlePartial purification of native HIV transmembrane protein gp41: generation of polyclonal and monoclonal antibodies.lld:pubmed
pubmed-article:3259140pubmed:affiliationProgram Resources, Inc., NCI-Frederick Cancer Research Facility, MD.lld:pubmed
pubmed-article:3259140pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:3259140pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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