[从抗流感病毒蛋白抗血清中分离及研究IgG的特性]
[Isolation and study of the properties of IgG from antisera to influenza virus proteins].
作者信息
Ivanova V T, Liubovtseva O V, Stafeeva O A, Savitskiĭ A P, Varecková E
出版信息
Vopr Virusol. 1987 Jan-Feb;32(1):39-44.
IgG to internal (NP, M) and external (HA, NA) proteins of influenza virus were isolated from immune rabbit sera using caprylic acid. The IgG retained their specificity and activity, worked in HI, lectin test, and enzyme-immunoassay. IgG migrated towards cathode in electrophoresis on acetate cellulose. Electrophoresis in polyacrylamide gel revealed a heavy chain (55,000) and a light chain (25,000) in IgG molecule. Different methods revealed changes in IgG structure after lyophilization. The possibility of recovering IgG from rat sera using caprylic acid was demonstrated. A comparative analysis of IgG recovered by means of caprylic acid as well as by polyethylene glycol or ammonium sulphate showed the IgG recovered with caprylic acid to contain less admixtures and to be suitable for use in immunological tests without additional purification.
使用辛酸从免疫兔血清中分离出针对流感病毒内部（核蛋白、基质蛋白）和外部（血凝素、神经氨酸酶）蛋白的IgG。这些IgG保留了它们的特异性和活性，可用于血凝抑制试验、凝集素试验和酶免疫测定。在醋酸纤维素电泳中，IgG向阴极迁移。聚丙烯酰胺凝胶电泳显示IgG分子中有一条重链（55,000）和一条轻链（25,000）。不同方法显示冻干后IgG结构发生了变化。证明了使用辛酸从大鼠血清中回收IgG的可能性。对通过辛酸以及聚乙二醇或硫酸铵回收的IgG进行的比较分析表明，用辛酸回收的IgG含有较少的杂质，无需进一步纯化即可用于免疫测试。
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