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Abstract：
A method is presented for locating protein antigenic determinants by analyzing amino acid sequences in order to find the point of greatest local hydrophilicity. This is accomplished by assigning each amino acid a numerical value (hydrophilicity value) and then repetitively averaging these values along the peptide chain. The point of highest local average hydrophilicity is invariably located in, or immediately adjacent to, an antigenic determinant. It was found that the prediction success rate depended on averaging group length, with hexapeptide averages yielding optimal results. The method was developed using 12 proteins for which extensive immunochemical analysis has been carried out and subsequently was used to predict antigenic determinants for the following proteins: hepatitis B surface antigen, influenza hemagglutinins, fowl plague virus hemagglutinin, human histocompatibility antigen HLA-B7, human interferons, Escherichia coli and cholera enterotoxins, ragweed allergens Ra3 and Ra5, and streptococcal M protein. The hepatitis B surface antigen sequence was synthesized by chemical means and was shown to have antigenic activity by radioimmunoassay.
摘要：
提出了一种通过分析氨基酸序列来定位蛋白质抗原决定簇的方法，以找到最大的局部亲水性点。这是通过为每个氨基酸分配数值(亲水性值),然后沿着肽链重复平均这些值来实现的。局部平均亲水性最高的点总是位于，或者紧邻，抗原决定簇.发现预测成功率取决于平均组长，六肽平均值产生最佳结果。该方法是使用12种蛋白质开发的，对其进行了广泛的免疫化学分析，随后用于预测以下蛋白质的抗原决定簇：乙型肝炎表面抗原，流感血凝素,禽鼠疫病毒血凝素,人组织相容性抗原HLA-B7,人干扰素,大肠杆菌和霍乱肠毒素，禾本科变应原Ra3和Ra5和链球菌M蛋白。乙型肝炎表面抗原序列是通过化学方法合成的，并通过放射免疫分析显示具有抗原活性。
