COMMON PEPTIDE EPITOPES IN GLYCOPHORIN AND THE ENDOTHELIAL SIALOGLYCOPROTEIN-GP60

被引:4
作者
SCHNITZER, JE
ULMER, JB
PALADE, GE
机构
[1] UNIV CALIF SAN DIEGO,SCH MED,DEPT OBSTET & GYNAECOL,DIV CELLULAR & MOLEC MED,LA JOLLA,CA 92093
[2] UNIV CALIF SAN DIEGO,SCH MED,INST BIOMED ENGN,LA JOLLA,CA 92093
[3] MERCK SHARP & DOHME LTD,DEPT CANC RES,W POINT,PA 19486
关键词
D O I
10.1016/0006-291X(92)91318-K
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Polyclonal anti-serum made against murine glycophorin gp3 (αgp) 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 β-elimination. When greater than 90% of the glycans of gp60 were removed, αgp 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 αgp immuno-globulins; these antibodies recognized gp60. Finally, αgp 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. © 1992.
引用
收藏
页码:1158 / 1165
页数:8
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