title: Partial purification and properties of the Epstein-Barr virus-associated nuclear antigen.
abstract: The Epstein-Barr virus (EBV)-associated nuclear antigen (EBNA) was purified 85-fold from a nuclear pellet derived from an EBV-transformed B lyphoblastoid cell line by a five-step procedure consisting of preparation of extract, heating at 80 degrees C in phosphate buffer, ammonium sulfate precipitation, preparative ultracentrifugation, and affinity chromatography on double-stranded DNA-cellulose. The purified complement fixing antigen specifically blocked the anticomplement immunofluorescence assay for EBNA. Several properties indicate a close association of EBNA with chromatin, viz. 1) precipitation of antigenic activity by phosphate buffer and subsequent thermal fractionation; 2) partial sensitivity of antigenic activity to DNase (but not to RNase) and restoration of activity by addition of calf thymus DNA; and 3) specific binding of EBNA to double-stranded DNA-cellulose. Other properties of EBNA, including its unusual heat stability, are described.
mesh_terms: D000974:Antibodies, Antinuclear; D000956:Antigens, Viral / Q000302:isolation & purification*; D002460:Cell Line; D002467:Cell Nucleus / Q000276:immunology*; D002472:Cell Transformation, Viral; D003168:Complement Fixation Tests; D003165:Complement System Proteins; D005455:Fluorescent Antibody Technique; D004854:Herpesvirus 4, Human / Q000276:immunology*
chemical_list: D000974:Antibodies, Antinuclear; D000956:Antigens, Viral; D003165:Complement System Proteins