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J Gen Virol 41 (1978), 447-457; DOI 10.1099/0022-1317-41-3-447
© 1978 Society for General Microbiology
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The Labelling of Galactose Residues in Hepatitis B Surface Antigen Glycoprotein

Jacinta Skelly, C. R. Howard and A. J. Zuckerman

Department of Medical Microbiology and WHO Collaborating Centre for Reference and Research on Viral Hepatitis, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT, U.K.

The 20 to 25 nm particles of hepatitis B surface antigen were purified from the serum of a carrier chimpanzee. Five major polypeptide species were revealed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Treatment of the particles with neuraminidase (EC 3.2.1.18 [EC] ) and galactose oxidase (EC 1.1.3.9 [EC] ) followed by reduction with tritiated sodium borohydride labelled galactose residues in a single glycoprotein with an apparent mol. wt. of 28000. The glycoprotein was not labelled when neuraminidase treatment was omitted, indicating that the galactose residues are in subterminal positions in the oligosaccharide chains. There was no significant incorporation of radiolabel into lipid. The serological activity of the antigen, as measured by a competitive double-antibody radioimmunoprecipitation assay, was not altered by the labelling procedure nor by exposure to neuraminidase alone.

Received 2 May 1978; accepted 13 June 1978.


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P Tiollais, P Charnay, and G. Vyas
Biology of hepatitis B virus
Science, July 24, 1981; 213(4506): 406 - 411.
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