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Analysis of Hepatitis B Surface Antigen Components Solubilized with Triton X-100

WHO Collaborating Centre for Reference and Research on Viral Hepatitis and Department of Medical Microbiology, London School of Hygiene and Tropical Medicine, Keppel Street, London W1CE 7HT

Three glycoproteins of intact hepatitis B surface antigen (HBsAg) with mol. wt. of 32000, 30000 and 28000 respectively were identified by reaction with ¹²⁵I-concanavalin A (Con A) after separation by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The antigen was effectively disrupted with Triton X-100 to produce a structure with a sedimentation coefficient of 3.9S. Affinity chromatography of disrupted HBsAg using concanavalin A-Sepharose 4B (Con A-Sepharose) resulted in two fractions. The first contained material which did not bind to the lectin and consisted of a single polypeptide of mol. wt. 64000. Further studies revealed this component to be serologically identical to serum albumin and to lack any affinity for antibody to HBsAg. A comparison of the tryptic peptide map of this polypeptide with that of purified serum albumin demonstrated identical amino-acid sequences. The second fraction contained material which bound to Con A and contained two polypeptides with mol. wt. of 28000 and 23000 respectively. HBsAg reactivity was associated with this fraction. This procedure allows the preparation of HBsAg sub-units in milligram quantities for further immunological studies.

Received 22 November 1978; accepted 22 February 1979.