Record Display for the EPA National Library Catalog


Main Title Radioimmunoassay Analysis of Baculovirus Granulins and Polyhedrins.
Author Summers, Max D. ; Hoops, Pepper ;
CORP Author Texas A and M Univ., College Station. Dept. of Entomology.;Health Effects Research Lab., Research Triangle Park, NC.
Year Published 1980
Report Number EPA-R-805232-01; EPA-600/J-80-258;
Stock Number PB81-192031
Additional Subjects Viruses ; Proteins ; Reprints ; Radioimmunoassay ; Autographa californica ; Rachiplusia ou ; Heliothis zea ; Heliothis armigera ; Trichoplusia ni ; Spodotera frugiperda ; Granulins ; Polyhedrins
Library Call Number Additional Info Location Last
NTIS  PB81-192031 Some EPA libraries have a fiche copy filed under the call number shown. 07/26/2022
Collation 12p
Granulin and polyhedrin proteins were purified by preparative sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis from the baculoviruses Autographa californica, Rachiplusia ou, Heliothis zea, Heliothis armigera, Trichoplusia ni, and Spodotera frugiperda. Antisera were raised against Autographa californica (Ac) polyhedrin and Trichoplusia ni (Tn) granulin and analyzed for homologous and heterologous immunoreactivity by immunodiffusion and radioimmunoassay (RIA). Ac polyhedrin and Tn granulin antisera recognized antigenic determinants on several baculovirus polyhedrin and granulin proteins even though the heterologous proteins had different immunoreactivities when compared by competition radioimmunoassay. Antigenic differences among granulin and polyhedrin proteins were also detected by altered slopes of the competition reaction curves. Antiserum raised against Ac polyhedrin which was purified in the presence of SDS was tested by competition RIA for its ability to detect and react with native polyhedrin produced in the infected TN-368 cells. Ac polyhedrin antiserum had similar if not identical ability to bind to native polyhedrin and to polyhedrin purified in the presence of SDS.