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SUMMARY: When concentrated purified influenza virus PR 8 was incubated at 37° with caseinase C in phosphate buffer at pH 7 and ionic strength 0.01 or 0.1, the neuraminidase activity was released from the virus particle and progressively destroyed. Under these conditions a material was released from virus which neutralized the haemagglutination inhibiting antibodies of anti-PR 8 rabbit serum. This material and neuraminidase, released by caseinase C, were both sedimented by centrifugation at 125,000 g. Neither was adsorbed to fowl red cells. After 4-hr incubation with caseinase C in phosphate buffer at pH 7 and ionic strength 0.1, the infectivity of influenza virus PR 8 suspension was considerably decreased, but its haemagglutinating activity was unchanged and remained bound to the virus particles. Under these conditions, most of the surface projections of the virus particles were removed.

Release of Influenza Virus Neuraminidase by Caseinase C of Streptomyces Albus G