Analysis of hepatitis B surface antigen components solubilized with Triton X-100.
J Gen Virol, 1979/9;44(3):679-89.
Skelly J, Howard CR, Zuckerman AJ
PMID: 93617
Impact factor: 5.141
Abstract
Three glycoproteins of intact hepatitis B surface antigen (HBsAg) with mol. wt. of 32 000, 30 000 and 28 000 respectively were identified by reaction with 125I-concanavalin A (Con A) after separation by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The antigen was effectively disrupted with Triton X-100 to produce a structure with a sedimentation coefficient of 3.9S. Affinity chromatography of disrupted HBsAg using concanavalin A-Sepharose 4B (Con A-Sepharose) resulted in two fractions. The first contained material which did not bind to the lectin and consisted of a single polypeptide of mol. wt. 64 000. Further studies revealed this component to be serologically identical to serum albumin and to lack any affinity for antibody to HBsAg. A comparison of the tryptic peptide map of this polypeptide with that of purified serum albumin demonstrated identical amino-acid sequences. The second fraction contained material which bound to Con A and contained two polypeptides with mol. wt. of 28000 and 23000 respectively. HBsAg reactivity was associated with this fraction. This procedure allows the prepartion of HBsAg sub-units in milligram quantities for further immunological studies.
MeSH terms
Animals; Chromatography, Affinity; Electrophoresis, Polyacrylamide Gel; Epitopes; Glycoproteins; Hepatitis B Surface Antigens; Hepatitis B virus; Humans; Molecular Weight; Pan troglodytes; Peptides; Polyethylene Glycols; Serum Albumin; Solubility
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