Structure of hepatitis B surface antigen. Correlation of subtype with amino acid sequence and location of the carbohydrate moiety.
Structure of hepatitis B surface antigen. Correlation of subtype with amino acid sequence and location of the carbohydrate moiety.
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DOI：
10.1016/s0021-9258(18)34034-1
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发表时间：
1982-09
期刊：
影响因子：
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通讯作者：
Darrell L. Peterson;Narapendra Nathy;Francisco GavilanesS
中科院分区：
文献类型：
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作者：
Darrell L. Peterson;Narapendra Nathy;Francisco GavilanesS
adw 和 ayw 亚型的乙型肝炎表面抗原 (HBsAg) 已从四种不同来源纯化。通过比较在不破坏 HBsAg 整体颗粒形态的条件下进行的胰蛋白酶水解产物，对这些抗原进行了比较。通过十二烷基硫酸钠存在下的聚丙烯酰胺凝胶电泳和高效液相色谱对所得肽进行比较，然后对分离的肽进行氨基酸分析和埃德曼降解。同样的技术也适用于在糖蛋白 gp-30 的碳水化合物部分用氚标记的 HBsAg。这些研究表明，蛋白质 p-25 和糖蛋白 gp-30 的残基 122-150 占据了 HBsAg 脂蛋白颗粒的暴露区域，并且在 gp-30 的情况下包含碳水化合物的主要附着位点。发现这两种亚型在该区域的两个特定位置上存在差异，表明这是该蛋白质的抗原重要区域。
Hepatitis B surface antigens (HBsAg) of both the adw and ayw subtypes have been purified from four different sources. These antigens have been compared by comparison of the products of tryptic hydrolysis performed under conditions which do not disrupt the overall particle morphology of HBsAg. The resultant peptides were compared by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and high performance liquid chromatography followed by amino acid analysis and Edman degradation of the isolated peptides. The same techniques were also applied to HBsAg which had been labeled with tritium in the carbohydrate moiety of the glycoprotein gp-30. These studies demonstrate that residues 122-150 of the protein p-25 and glycoprotein gp-30 occupy an exposed region of the HBsAg lipoprotein particle and contain the major attachment site for carbohydrate in the case of gp-30. The two subtypes were found to differ at two specific positions in this region, suggesting that this is an antigenically important area of the protein.