6533b7d8fe1ef96bd126acd7

RESEARCH PRODUCT

Association of hepatitis Be antigen (HBeAg) with the core of the hepatitis B virus (HBcAg).

J. SlusarczykK.-h. Meyer Zum BoschenfeldeGeorg Hess

subject

DNA polymerasePronaseDNA-Directed DNA Polymerasemedicine.disease_causeGuanidinesHepatitis B Antigenschemistry.chemical_compoundAntigenmedicineHumansHepatitis B e AntigensGuanidineGuanidineHepatitisHepatitis B virusHepatologybiologyChemistryvirus diseasesSodium Dodecyl Sulfatemedicine.diseaseHepatitis BVirologyHepatitis B Core Antigensdigestive system diseasesHBcAgHBeAgPronasebiology.protein

description

— Three substances (pronase E, sodium dodecylsulfate (SDS) and guanidine hydrochloride) with different chemical actions partially convert HBcAg to HBeAg. This process retains the integrity of the HBcAg particle, which was not different between HBcAg subpopulations, and does not generate HBcAg or HBeAg sub-units. DNA polymerase activity was destroyed by SDS and guanidine hydrochloride, but not by pronase E. Serum HBeAg could not be converted into HBcAg, suggesting that this might be an irreversible process. The data are consistent with the assumption that HBcAg and HBeAg are coded for by the same gene (C gene of the HBV-DNA).

10.1111/j.1600-0676.1985.tb00015.xhttps://pubmed.ncbi.nlm.nih.gov/3982243