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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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Monoclonal antibodies against Taka virus, a variant of Newcastle disease virus (NDV), were produced to compare the antigenicites of several avian paramyxoviruses including NDV. It was also used to study the activesite(s) of haemagglutin (HA) and neuraminidase activities of NDV.
Five independent hybrid cell lines, which produced monoclonal antibodies against haemagglutinin-neuraminidase (HN) molecule of Taka virus, were established. From the results of the cross haemagglutination-inhibition (HI) test the monoclonal antibodies, the HN molecule of Taka virus seemed to have at least three different antigenic determinats; one was specific for all NDV strain tested, the second was only for Taka virus and the third was for Take virus, Bangor and Yucaipa. Furthermore the differences in the ratio of HI to neuraminidase-inhibition titers suggested that the active sites involved in HA and neuraminidase activities might be different from each other. However, since each of five monoclonal antibodies was not especially specific for either HA or neuraminidase, the possibility that a single active site on the HN molecule may be responsible for both activities has not been excluded.
Five independent hybrid cell lines, which produced monoclonal antibodies against haemagglutinin-neuraminidase (HN) molecule of Taka virus, were established. From the results of the cross haemagglutination-inhibition (HI) test the monoclonal antibodies, the HN molecule of Taka virus seemed to have at least three different antigenic determinats; one was specific for all NDV strain tested, the second was only for Taka virus and the third was for Take virus, Bangor and Yucaipa. Furthermore the differences in the ratio of HI to neuraminidase-inhibition titers suggested that the active sites involved in HA and neuraminidase activities might be different from each other. However, since each of five monoclonal antibodies was not especially specific for either HA or neuraminidase, the possibility that a single active site on the HN molecule may be responsible for both activities has not been excluded.
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