The isolation and purification of pre-S2 containing hepatitis B virus surface antigen by chemical affinity chromatography

Appl Biochem Biotechnol. 1987 Oct;15(3):255-63. doi: 10.1007/BF02798453.

Abstract

A simple, rapid, and efficient method was developed to isolate and purify pre-S2 containing HBsAgs from the plasma of a single chronic carrier of HBsAg (adw) by ammonium sulfate fractionation, hydroxyapatite column chromatography, and polymerized human serum albumin-affinity column chromatography. About 500 micrograms of pre-S2 containing HBsAg was obtained from 140 mL of plasma containing 4,200 micrograms of HBsAg. Two purified pre-S2 containing HBsAgs were analyzed by SDS-polyacrylamide gel electrophoresis and their molecular weights were determined to be 31,000 and 68,000 respectively. No significant amount of HBsAg or its derivative was detected in the final product.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography / methods
  • Chromatography, Affinity / methods
  • Durapatite
  • Electrophoresis, Polyacrylamide Gel
  • Hepatitis B Surface Antigens / isolation & purification*
  • Humans
  • Hydroxyapatites
  • Molecular Weight
  • Protein Precursors / isolation & purification*
  • Serum Albumin

Substances

  • Hepatitis B Surface Antigens
  • Hydroxyapatites
  • Protein Precursors
  • Serum Albumin
  • presurface protein 2, hepatitis B surface antigen
  • Durapatite