<Emphasis Type="Italic">N</Emphasis>-glycosylation profile of the protective chimeric antibody ch14D5a against tick-borne encephalitis virus |
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| Authors: | I K Baykov A L Matveev I G Kondratov N V Tikunova |
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| Institution: | 1.Institute of Chemical Biology and Fundamental Medicine, Siberian Branch,Russian Academy of Sciences,Novosibirsk,Russia;2.Limnological Institute, Siberian Branch,Russian Academy of Sciences,Irkutsk,Russia |
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| Abstract: | The glycosylation profile of the chimeric antibody ch14D5a against the tick-borne encephalitis virus has been analyzed. It has been found that the ch14D5a antibody is completely N-glycosylated at the asparagine 297 residue of both heavy chains, and the major glycoforms correspond supposedly to glycoforms G0F, G1F, and G2F, which are most typical for human immunoglobulins IgG and for antibodies secreted by CHO cells. |
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