Gel filtration of hepatitis B surface antigen: increased size of the native particle.
The Stokes radius of umpurified hepatitis B antigen (HBSAg) was determined by chromatography on a carefully calibrated Sepharose 4B column. A value of 14-2 nm was found by this procedure, contrasting with a published value of II nm for purified, pepsin-treated HBSAg. Chromatography at pH 3 appeared to reduce the Strokes radius of HBSAg to II nm. Evidence is presented to show that serum proteins adsorbed to HBSAg can be removed with pepsin or acid.
Gel filtration of hepatitis B surface antigen: increased size of the native particle. The Stokes radius of umpurified hepatitis B antigen (HBSAg) was determined by chromatography on a carefully calibrated Sepharose 4B column. A value of 14-2 nm was found by this procedure, contrasting with a published value of II nm for purified, pepsin-treated HBSAg. Chromatography at pH 3 appeared to reduce the Strokes radius of HBSAg to II nm. Evidence is presented to show that serum proteins adsorbed to HBSAg can be removed with pepsin or acid.