PURIFICATION OF ANTIBODIES TO INFLUENZA A VIRUS STRUCTURAL PROTEINS BY AFFINITY CHROMATOGRAPHY, AND THEIR PARTICIPATION IN HAEMAGGLUTINATION-INHIBITION, NEUTRALIZATION AND ENZYME-LINKED IMMUNOSORBENT ASSAY

被引：6

作者：

WATANABE, H ^{[1
]}

POLLETT, M ^{[1
]}

MACKENZIE, JS ^{[1
]}

机构：

[1] QUEEN ELIZABETH MED CTR,DEPT MICROBIOL,NEDLANDS 6009,W AUSTR.,AUSTRALIA

来源：

AUSTRALIAN JOURNAL OF EXPERIMENTAL BIOLOGY AND MEDICAL SCIENCE | 1979年 / 57卷 / JUN期

关键词：

D O I：

10.1038/icb.1979.33

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

Affinity chromatography was used to purify rabbit antibodies to common and strain-specific antigeneic determinants of haemagglutinin, to neuraminidase, and to a combination of the internal proteins of influenza A viruses. The purity of the antibodies was assessed by haemagglutination-inhibition, enzyme-linked immunosorbent assay (ELISA) and competition ELISA. The antibodies were examined for their participation in neutralization and haemagglutination-inhibition assays, and in ELISA. ELISA was found to be the most sensitive technique for detecting antibodies. Antibodies to the common and strain-specific determinants of haemagglutinin were shown to participate in neutralization assays and ELISA, but only those antibodies to the common determinants were detected by haemagglutination-inhibition.

引用

页码：303 / 312

页数：10