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• W211448333 abstract "Research Article1 October 1984free access An amphipathic sulphated glycoconjugate of Leishmania: characterization with monoclonal antibodies. E. Handman E. Handman Search for more papers by this author C.L. Greenblatt C.L. Greenblatt Search for more papers by this author J.W. Goding J.W. Goding Search for more papers by this author E. Handman E. Handman Search for more papers by this author C.L. Greenblatt C.L. Greenblatt Search for more papers by this author J.W. Goding J.W. Goding Search for more papers by this author Author Information E. Handman, C.L. Greenblatt and J.W. Goding The EMBO Journal (1984)3:2301-2306https://doi.org/10.1002/j.1460-2075.1984.tb02130.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info A major glycoconjugate of Leishmania tropica major identified by two monoclonal antibodies was shown to be an externally oriented, amphipathic membrane antigen shed into the culture medium in which the parasites grow. This molecule could be labelled metabolically with [3H]glucose, [3H]galactose, [32P]phosphate and [35S]sulphate. It migrated as a polydisperse band upon electrophoresis in SDS-polyacrylamide gels, spanning the region of the gel corresponding to an apparent mol. wt. of 20 000-67 000 daltons. An apparently identical family of molecules could be labelled on the surface of living promastigotes using galactose oxidase and [3H]-sodium borohydride. This molecule was shown to be released into the supernatant over a period of several hours. Detection of the 3H- or 35S-labelled molecule required several days exposure of autoradiographs, but a novel blotting technique using nitrocellulose coated with monoclonal antibody allowed rapid detection of the molecule in charge shift electrophoresis, Western blotting and dot blotting. The electrophoretic mobility of the glycoconjugate in agarose relative to its mobility in Triton X-100 was increased in the presence of deoxycholate, and decreased in the presence of cetyl trimethyl-ammonium bromide, indicating amphipathic properties consistent with insertion into the lipid bilayer of the membrane. Using the dot-blotting technique the glycoconjugate was detected in all virulent and avirulent clones of LRC-L137 and in two additional isolates of L. tropica major (LRC-L287 and LRC-L251), but not in L. donovani or L. mexicana, consistent with the previously described specificity of the antibodies. However, the general approaches used in this paper showed that L. donovani (LRC-L52) and L. mexicana (LRC-L94) synthesize a similar, but antigenically distinct glycoconjugate. Previous ArticleNext Article Volume 3Issue 101 October 1984In this issue RelatedDetailsLoading ..." @default.
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• W211448333 title "An amphipathic sulphated glycoconjugate of Leishmania: characterization with monoclonal antibodies." @default.
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• W211448333 doi "https://doi.org/10.1002/j.1460-2075.1984.tb02130.x" @default.
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