Abstract
Highly purified influenza virus was degraded using anionic and non-ionic detergents. Best results were obtained using the non-ionic detergent Triton N 101. Tests showed that virus extracts contained neuraminidase and a substance that reacted specifically with rabbit antibody to virus haemagglutinin (specific serum blocking substance). Haemagglutination-inhibiting antibody was produced when virus extracts were inoculated into guinea-pigs. Immunodiffusion tests showed that extracts were complex. Host-specific material was regularly found. Under appropriate conditions S-antigen was detected as a single line pattern component. Two or more virus-specific materials were also present. One of these was probably neuraminidase and the other the specific serum blocking substance.