Biochemical and biophysical properties of hepatitis B core particles derived from Dane particles and infected...

Hepatitis B core antigen (HBcAg) was purified from Dane particles and from infected hepatocytes. An identical isoelectric pH of 4.0 was determined for labeled preparations of both Dane-derived and liver-derived HBcAg. Unlabeled liver-derived HBcAg demonstrated a lower isoelectric pH of 3.7. Molecular weight determinations by Sepharose 4B column chromatogrpahy revealed that liver-derived HBcAg had a molecular weight of 8.5-9.0 X 10(6) daltons. The sedimentation coeficient of both Dane- and liver-derived HBcAg was found to be 124S. PAGE revealed that iodinated HBcAg derived from Dane particles was very similar in polypeptide structure to HBcAg derived from infected liver tissue. Twelve polypeptides were resolved from Dane core particles, and seven to nine were resolved from liver core particles. Several of the polypeptides in both preparations co-migrated with iodinated hepatitis B surface antigen (HBsAg). However, three polypeptides (mol. wt. 88,000, 79,000 and 59,000) were found in both Dane- and liver-derived HBcAg but not in HBsAg, which suggests that these polypeptides are HBcAg-specific. Endogenous DNA polymerase activity was observed in both Dane- and liver-derived core particles.