Common peptide epitopes in glycophorin and the endothelial sialoglycoprotein gp60. |
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Authors: | J E Schnitzer J B Ulmer G E Palade |
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Affiliation: | Dept. of Medicine, Univ. Calif.- San Diego School of Medicine, La Jolla 92093-0651. |
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Abstract: | Polyclonal anti-serum made against murine glycophorin gp3 (alpha gp) recognizes the endothelial albumin binding glycoprotein, gp60. In this study, we investigated the nature (peptide vs. carbohydrate) of the common epitope. First, a new technique was developed to remove oligosaccharides from glycoproteins that were first immobilized on filters and then subjected to beta-elimination. When greater than 90% of the glycans of gp60 were removed, alpha gp still recognized gp60 without apparent loss of affinity. Second, we used brefeldin A to accumulate unglycosylated glycophorin precursors in order to affinity-purify peptide-specific alpha gp immuno-globulins; these antibodies recognized gp60. Finally, alpha gp recognized from in vitro translations a 48 kDa putative polypeptide precursor of gp60. These different approaches indicate that gp60 and gp3 have at least one common epitope in their peptide backbones. |
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