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polypeptide p/epatite
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6 risultati
Relationship of large hepatitis B surface antigen polypeptide to human serum albumin.
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A significant proportion (20 to 40%) of highly purified 22-nm hepatitis B surface antigen (HBsAg) particles contain human serum albumin (HSA) as demonstrated by specific precipitation of radioiodinated particles by anti-HSA. Preparations of the isolated major HBsAg polypeptides (P-1, P-2, and P-6)
Proteins of hepatitis B surface antigen.
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Purified 22-nm forms of hepatitis B surface antigen (Hbsag) representing the three major antigenic subtypes (adw, ayw, and adr) were analyzed for their constituent polypeptides by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. No consistent difference in either the number or relative
Antigenicity of the major polypeptides of hepatitis B surface antigen (HBsAg).
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The major polypeptides (P-1, P-2, and P-6) of HBsAg were isolated from purified preparations of 22-nm HBsAg particles, iodinated, and analyzed by double-antibody radioimmunoprecipitation assays for the presence of hepatitis B virus (HBV)-specific antigens. Each polypeptide fraction contained both
Antigenic and structural relationships of the surface antigens of hepatitis B virus, ground squirrel hepatitis virus, and woodchuck hepatitis virus.
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The surface antigens of human hepatitis B (HBsAg), ground squirrel hepatitis (GSHsAg), and woodchuck hepatitis (WHsAg) viruses were compared serologically, and their major polypeptides were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and tryptic peptide mapping. Results
Immunochemistry of hepatitis B surface antigen (HBsAg): preparation and characterization of antibodies to the constituent polypeptides.
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The structural polypeptides of HBsAg were shown to be immunogenic in guinea pigs. Purified 22-nm forms of the ad and any subtypes of HBsAg were solubilized under reducing conditions and electrophoresed in SDS-polyacrylamide gels. Individual polypeptides isolated from both HBsAg/ad and HBsAg/ay
Further studies on production and characterization of HBsAg derived from a human hepatoma cell line (PLC/PRF/5).
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Four aspects for the use of PLC/PRF/5 cell line as an alternative source of HBsAg for hepatitis B vaccine production were assayed in this study: improvement in HBsAg production with chemical inducers, tests for the presence of hepatitis B virions, antigenic topology of HBsAg polypeptides and
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