Immunochemical and Morphological Studies of Hepatitis B Core Antigen Isolated from the Nuclei of Hepatocytes

Abstract

Immunochemical and morphological properties of hepatitis B core antigen (HB_e Ag) were studied Inmtranuclearparticles isolated from human liver. Immunochemical integrity of the purified particles was indicated in the production by guinea pigs of antibody to HB_e Ag (anti-HBj) that was immunochenti{ally identical to human anti-Hf_e. The HB_e Ag particles were 27–30 nm in diameter, displayed apparent icosahedral symmetry, and consisted of distinct subunits. The susceptibility of HB_e Ag particles to proteolytic and glycolytic enzymes indicated the presence of proteins and glycoproteins. The structural integrity of core particles depended on disulfide, hydrophobic, and hydrogen bonds, and immunological activity relied on intact sulfhydryl groups. Agents active against lipids did not affect immunological reactivity or core structure, as seen by electron microscopy.