Immunoaffinity purification and receptor assay for polymerized human serum albumin of pre-S2 peptide on hepatitis B virus

Abstract

Recombinant pre-S2 peptide was purified to apparent homogeneity from E. coll by immunoaffinity chromatography using monoclonal an仕body and studied for its binding characteristics with monoclonal an仕body and pHSA (polymerized human serum albumin). A simple and senskive assay method for detecting the activity of pHSA receptor on pre-S2 peptide of hepatitis B virus surface antigen (HBsAg) has been developed using pre-S2-分-galactosidase fusion protein. The assay can be used for determining pre-S2 or factors neutralizing pHSA receptor activity. The sensitivity of the assay is about 10 to 100 pmol of pre-S2.