Abstract
Summary Hydrophobic chromatography was used to purify hepatitis B surface antigen (HBsAg) particles from human serum and from human and mouse HBsAg-producing cell lines. The particles were retained on a hexyl-agarose column, while most of the contaminating proteins did not bind. They were eluted by a high-ionic strength buffer (NaCl 1 M) containing ethylene glycol 8.5 M. Two major polypeptides, P1 and P2—coded by gene S—and several other polypeptides with higher molecular weight, were present in the particles eluted from the column.
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