High frequency antigens of human erythrocyte membrane sialoglycoproteins, V. Characterization of the Gerbich blood group antigens: Ge2 and Ge3.

High frequency antigens of human erythrocyte membrane sialoglycoproteins, V. Characterization of the Gerbich blood group antigens: Ge2 and Ge3.
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人红细胞膜唾液酸糖蛋白的高频抗原,V。Gerbich 血型抗原的表征:Ge2 和 Ge3。

DOI:
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发表时间:
1987
期刊:
Biological Chemistry Hoppe-Seyler
影响因子:
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通讯作者:
J. Cartron
J. Cartron
中科院分区:
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文献类型:
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作者:
W. Dahr;S. Kiedrowski;D. Blanchard;P. Hermand;J. Moulds;J. Cartron

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采用来自罕见的Ge: -1、-2、-3或Ge: -1、-2、3个体的14种不同的同种抗体,研究了人Gerbich血型系统主要高频抗原(Ge2和Ge3)的分子特性。从正常红细胞(表型Ge: 1、2、3)中提取的各种糖蛋白(唾液糖蛋白)的修饰、分离或碎片化产物用于血凝抑制试验。抗原的位置也通过用十二烷基硫酸聚丙烯酰胺凝胶电泳将蛋白质与硝化纤维素分离,并用125i标记的蛋白质g检测结合抗体来研究。发现Anti-Ge3靶向糖蛋白C的一个区域,该区域围绕着一个位于48号位置的胰蛋白酶裂解位点,以及糖蛋白D的一个类似区域,其结构尚不清楚。根据化学修饰判断,Ge3表位涉及NeuAc残基,可能代表部分与糖蛋白C的丝氨酸42、蛋氨酸、天冬氨酸或谷氨酸、色氨酸和/或精氨酸残基相连的碳水化合物单元。发现Ge2表位位于糖蛋白D的一个由约20-30个氨基酸残基组成的色氨酸糖肽上。附着在丝氨酸/苏氨酸连接的低聚糖上的NeuAc残基参与了Ge2决定因子。利用免疫印迹技术,还可以证明Ge3: - 1,2,3细胞中的“新”糖蛋白携带Ge3抗原。
The molecular properties of the major, high-frequency antigens (Ge2 and Ge3) of the human Gerbich blood group system were investigated using 14 different alloantibodies from rare Ge: -1,-2,-3 or Ge: -1,-2,3 individuals. Various modification, fractionation or fragmentation products of glycophorins (sialoglycoproteins) from normal erythrocytes (phenotype Ge: 1,2,3) were used in hemagglutination inhibition assays. The location of the antigens was also studied by blotting of proteins, separated by dodecyl sulfate polyacrylamide gel electrophoresis, to nitrocellulose and detection of bound antibodies by 125I-labelled protein G. Anti-Ge3 was found to be directed against a region of glycophorin C that surrounds a tryptic cleavage site at position 48 and a similar region of glycophorin D whose structure is not yet known. NeuAc residue(s), probably representing part(s) of a carbohydrate unit attached to serine42 of glycophorin C, methionine, aspartic or glutamic acid, tryptophan and/or arginine residue(s) are involved in the Ge3 epitopes, as judged from chemical modification. The Ge2 epitopes were found to be located on a tryptic glycopeptide from glycophorin D comprising about 20-30 amino-acid residues. NeuAc residue(s), attached to serine-/threonine-linked oligosaccharide(s), are involved in the Ge2 determinants. Using the immunoblotting technique, it could also be shown that the 'new' glycophorin in Ge: -1,-2,3 cells carries the Ge3 antigen.