Adsorption properties of different hepatitis B virus related antigens (HBsAg, HBcAg, HBeAg) on octanohydrazide-Sepharose 4B.
Chromatography of plasma containing hepatitis B virus and partially purified viral antigens on a hydrophobic gel derivative (octanohydrazide-Sepharose 4B) revealed that HbsAg and HbcAg were adsorbed to the gel in 0.75 mol/l ammonium bicarbonate and eluted by a detergent, Berol. HBeAg in a purified HBcAg preparation from human liver, but not HBeAg in plasma, was bound to the gel. Furthermore, HBeAg in the HBcAg preparation, but not HBeAg in plasma, lost its antigenic reactivity in the presence of Berol, indicating that the two HBeAgs were present in different molecular configurations. However, HBeAg could be released from HBV (HBcAg) and form a component which sedimented slowly and was immune-reactive in the presence of the detergent. The results contribute to knowledge of the interrelationship between hepatitis B-related antigens and indicate that chromatography on hydrophobic gel derivatives can be used not only for the purification (and removal) of HBsAg but also of HBcAg.
D000327:Adsorption; D002499:Centrifugation, Density Gradient; D002847:Chromatography, Agarose; D006511:Hepatitis B Antigens / Q000032:analysis*; D006512:Hepatitis B Core Antigens / Q000032:analysis*; D006514:Hepatitis B Surface Antigens / Q000032:analysis*; D006513:Hepatitis B e Antigens / Q000032:analysis*; D006801:Humans; D012685:Sepharose / Q000031:analogs & derivatives*
D006511:Hepatitis B Antigens; D006512:Hepatitis B Core Antigens; D006514:Hepatitis B Surface Antigens; D006513:Hepatitis B e Antigens; C042409:octanohydrazide-sepharose 4B; D012685:Sepharose