从流感病毒血凝素中分离出的一种抗原糖蛋白的特性
Properties of an antigenic glycoprotein isolated from influenza virus hemagglutinin.
作者信息
Eckert E A
出版信息
J Virol. 1973 Feb;11(2):183-92. doi: 10.1128/JVI.11.2.183-192.1973.
Abstract
A purified antigen, HABA protein, has been derived from influenza virus concentrates by extraction with denaturing solvents. The protein lacks hemagglutinating activity but binds completely strain-specific, hemagglutination-inhibiting antibodies and induces neutralizing antibodies in experimental animals. Physicochemical characterization of HABA protein identifies it as a single homogeneous glycoprotein with a molecular weight of 78,000. On dissociation with guanidine or sodium dodecyl sulfate, in the presence of reducing agents, only one size of polypeptide with a molecular weight of the order of 40,000 is characteristic of the preparations. The data indicate that HABA protein is a dimer of HA(1) polypeptide of the influenza virus hemagglutinin substructure, and that only trace amounts of other polypeptides are present.
摘要
一种纯化抗原，即HABA蛋白，是通过用变性溶剂从流感病毒浓缩物中提取得到的。该蛋白缺乏血凝活性，但能完全结合菌株特异性的血凝抑制抗体，并在实验动物中诱导中和抗体。HABA蛋白的物理化学特性表明它是一种分子量为78,000的单一均一糖蛋白。在有还原剂存在的情况下，用胍或十二烷基硫酸钠解离时，制剂的特征是只有一种分子量约为40,000的多肽。数据表明，HABA蛋白是流感病毒血凝素亚结构的HA(1)多肽的二聚体，并且只存在痕量的其他多肽。
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