Examination of the Polypeptides of Hepatitis B Surface Antigen

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Abstract
When the polypeptides of hepatitis B surface antigen (HBsAg) were examined by SDS[sodium dodecyl sulfate]-polyacrylamide gel electrophoresis under a variety of conditions, anomalous results were due to variable and at times incomplete dissociation of polypeptides after boiling with 1% SDS and reducing agent, reaggregation of solubilized material under certain electrophoretic conditions and during laboratory manipulations and the variable presence of additional components in HBsAg prepared from certain individual [human] donors. When these factors were taken into account, 2 major components were consistently identified by discontinuous buffer polyacrylamide gel electrophoresis, of apparent MW 60,000-70,000 and 12,000-14,000. In view of the demonstrated limitations of this technique in examining HBsAg polypeptides, alternative methods are necessary to confirm the true MW of the unique virus-specified amino acid sequence present.