| Abstract: | Using a monoclonal IgM antibody (anti-HBs) to hepatitis B surface antigen (HBsAg) in a radioimmunoassay for hepatitis B, we have detected high binding activity in human serum that was unreactive in assays employing conventional anti-HBs reagents. The binding material was isolated from serum by affinity chromatography on monoclonal IgM anti-HBs, and comparison of the material with HBsAg (by sodium dodecyl sulfate/polyacrylamide gel electrophoresis) demonstrated that the two shared several similar polypeptides. Furthermore, comparison of the binding properties of HBsAg and concentrated monoclonal immunoreactive material with conventional and monoclonal anti-HBs reagents demonstrated some antigenic crossreactivity. The molecular weight of the monoclonal immunoreactive material was approximately 2 X 10(6). Immunoprecipitation of the material with monoclonal IgM antibodies and examination by electron microscopy revealed clumped and "spiculated" particles that resembled 22-nm hepatitis B particles coated with the same antibody. Thus, this study suggests that the high-binding-activity material, detected in serum only by the monoclonal radioimmunoassay, is not identical with HBsAg, but it shares some common properties. |
