Hepatitis B Antigen: Antigenic Sites Related to Human Serum Proteins Revealed by Affinity Chromatography
AUTOR(ES)
Neurath, A. Robert
RESUMO
Hepatitis B antigen-associated particles, isolated from sera of antigen carriers, were submitted to affinity chromatography on columns of insolubilized antibodies to normal human plasma. The particles adsorbed to the immunosorbent at pH 7.2 and were subsequently eluted at pH 2.2. Exposure of the particles to 8 M urea, 5 M KI, pH 2.2, detergents, organic solvents, or proteolytic enzymes failed to prevent their subsequent adsorption to the immunosorbent. This suggests that antigenic determinants related to human plasma proteins are constituent components of hepatitis B antigen-associated particles. These determinants are distinct from the group-specific (a) and subtype-specific (d or y) sites of the hepatitis B antigen and appear to be related to antigenic specificities on prealbumin, albumin, apolipoproteins C and D, and the γ-chain of immunoglobulin G.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=388527Documentos Relacionados
- Monoclonal radioimmunoassays for hepatitis B surface antigen: demonstration of hepatitis B virus DNA or related sequences in serum and viral epitopes in immune complexes.
- Proteins of hepatitis B surface antigen: amino acid compositions of the major polypeptides.
- Hepatitis B Core Antigen: Immunology and Electron Microscopy
- Failure to detect polyalbumin-binding sites on the woodchuck hepatitis virus surface antigen: implications for the pathogenesis of hepatitis B virus in humans.
- Relationship of large hepatitis B surface antigen polypeptide to human serum albumin.