[Characterization of Yersinia pestis fibrinolysin using monoclonal antibody].
Immunochemical identity of Y. pestis fibrinolysin and coagulase is demonstrated using monoclonal antibodies. These substances are proven to exist as complex proteins with two independent activities. Possible causes of this phenomenon are discussed. Coagulase antigenic determinants are involved in specific fluorescence of Y. pestis cells grown at 28 degrees C. A new original method for screening the hybridomas producing monoclonal antibodies is proposed, based on inhibition of the functional activity of antigen.
Fedorova
V A
VA
Devdariani
Z L
ZL
D000907:Antibodies, Bacterial / Q000276:immunology; D000911:Antibodies, Monoclonal / Q000276:immunology; D001426:Bacterial Proteins / Q000032:analysis / Q000276:immunology; D000939:Epitopes / Q000276:immunology; D005341:Fibrinolysin / Q000032:analysis* / Q000276:immunology; D013379:Substrate Specificity; D015010:Yersinia pestis / Q000201:enzymology* / Q000276:immunology
D000907:Antibodies, Bacterial; D000911:Antibodies, Monoclonal; D001426:Bacterial Proteins; D000939:Epitopes; D005341:Fibrinolysin