Immunochemistry and polypeptide composition of hepatitis B core antigen (HBc Ag).
Core particles were isolated from a nuclear extract of a hepatitis B-infected liver labeled with 125I by using chloramine-T and further purified by rate zonal sedimentation on sucrose gradients. Iodinated HBcAg was used as a ligand in a sensitive double-antibody radioimmunoprecipitation (RIP) assay for antibody to HBcAg. The specificity of the RIP reaction was evaluated using defined anti-HBc sera and paired sera from six well-documented cases of hepatitis B infection. The polypeptide composition of the iodinated antigen was examined by SDS-polyacrylamide gel electrophoresis of solubilized complexes of 125I-HBcAg and anti-HBc. Two major polypeptides with apparent m.w. of 17,000 and 35,000 daltons were observed and designated as cP-1 and cP-2, respectively.
D000914:Antibodies, Viral / Q000032:analysis; D000939:Epitopes; D006509:Hepatitis B / Q000276:immunology; D006512:Hepatitis B Core Antigens / Q000302:isolation & purification; D006801:Humans; D007120:Immunochemistry; D008970:Molecular Weight; D010455:Peptides / Q000276:immunology / Q000302:isolation & purification; D011863:Radioimmunoassay; D014764:Viral Proteins / Q000276:immunology / Q000302:isolation & purification
D000914:Antibodies, Viral; D000939:Epitopes; D006512:Hepatitis B Core Antigens; D010455:Peptides; D014764:Viral Proteins