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Radioimmunoassay analysis of baculovirus granulins and polyhedrins

Identifieur interne : 004F66 ( Main/Exploration ); précédent : 004F65; suivant : 004F67

Radioimmunoassay analysis of baculovirus granulins and polyhedrins

Auteurs : Max D. Summers [États-Unis] ; Pepper Hoops [États-Unis]

Source :

RBID : ISTEX:7C4E286BD3F79303C61798D0AA6D5597EBDBEA73

English descriptors

Abstract

Abstract: 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 Spodoptera 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.

Url:
DOI: 10.1016/0042-6822(80)90128-2


Affiliations:


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<term>Antiserum</term>
<term>Assay</term>
<term>Baculovirus</term>
<term>Baculoviruses</term>
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<term>Nuclear polyhedrosis viruses</term>
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<term>Polyhedron</term>
<term>Polyhedrosis</term>
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<term>Radioimmunoassay</term>
<term>Room temperature</term>
<term>Sfgv</term>
<term>Sfgv granulin</term>
<term>Tngv</term>
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<term>Tnsnpv polyhedrin</term>
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<div type="abstract" xml:lang="en">Abstract: 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 Spodoptera 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.</div>
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