The characterization and purification of DNA binding proteins present within herpes simplex virus infected cells using monoclonal antibodies.
Hybridomas secreting monoclonal antibodies against herpes simplex virus (HSV) DNA binding proteins (DBP) have been produced. Five HSV DBP have been characterized according to molecular weight, affinity for DNA, kinetic class and localization within the infected cell. By preparing an immunoadsorbent column from antibody TI8, its specific DBP was purified to apparent homogeneity. The purified DBP retained the ability to bind to DNA.
D000818:Animals; D000911:Antibodies, Monoclonal; D002460:Cell Line; D002472:Cell Transformation, Viral; D002482:Cellulose / Q000031:analogs & derivatives / Q000378:metabolism; D006224:Cricetinae; D004247:DNA / Q000031:analogs & derivatives / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000302:isolation & purification*; D005455:Fluorescent Antibody Technique; D007700:Kinetics; D008970:Molecular Weight; D011499:Protein Processing, Post-Translational; D018139:Simplexvirus / Q000235:genetics*
D000911:Antibodies, Monoclonal; D004268:DNA-Binding Proteins; C033190:DNA-cellulose; D002482:Cellulose; D004247:DNA