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• W2022251854 endingPage "5199" @default.
• W2022251854 startingPage "5195" @default.
• W2022251854 abstract "We describe the isolation and cloning of two integral membrane protein antigens of Plasmodium falciparum. The antigens were isolated by Triton X-114 temperature-dependent phase separation, electrophoretically transferred to nitrocellulose, and used to affinity-purify monospecific human antibodies. These antibodies were used to isolate the corresponding cDNA clones from a phage lambda gt11-Amp3 cDNA expression library. Clone Ag512 corresponds to a Mr 55,000 merozoite rhoptry antigen, and clone Ag513 corresponds to a Mr 45,000 merozoite surface antigen. Both proteins can be biosynthetically labeled with [3H]glucosamine and [3H]myristic acid, suggesting that they may be anchored in membranes via a glycosylphosphatidylinositol moiety. Similarities in the C-terminal sequences of the Mr 45,000 merozoite surface antigen and the Trypanosoma brucei variant surface glycoproteins provides further evidence that this antigen has a glycosylphosphatidylinositol anchor." @default.
• W2022251854 created "2016-06-24" @default.
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• W2022251854 date "1988-07-01" @default.
• W2022251854 modified "2023-09-23" @default.
• W2022251854 title "Identification of two integral membrane proteins of Plasmodium falciparum." @default.
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• W2022251854 doi "https://doi.org/10.1073/pnas.85.14.5195" @default.
• W2022251854 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/281715" @default.
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