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Host Components in Hepatitis B Antigen

Australia Antigen Reference Laboratory, Department of Bacteriology, Edinburgh University Medical School, Teviot Place, Edinburgh, EH8 9AG, U.K.

Purified [¹²⁵I]-labelled 20 to 25 nm hepatitis B antigen particles were found to give low affinity immunoprecipitation reactions with antisera to several normal serum components, which were immunologically distinct from the reaction due to the classical hepatitis B antigen surface determinant. These additional antigenic determinants were acid-stable and tightly bound to the particles; they could not be released by treatment with Tween 80 or ether, but were removed by protease digestion with the preservation of particle integrity. It was not possible to distinguish whether they were due to the presence of trace amounts of partly denatured serum components, or to a weak cross-reaction with antigens present in normal serum. The implications of this finding for hepatitis B antigen and antibody detection in sensitive assays are discussed. No evidence was found for native antigenic material, present in normal serum or normal liver cells, being integral to the structure of these particles.

Received 6 August 1974; accepted 6 January 1975.