1887

Abstract

Summary

A polypeptide of 21500 mol. wt., structurally associated with hepatitis B virus core particles, was shown to have two kinds of HBeAg antigenicity (HBeAg/1 and HBeAg/2). This was revealed by transferring a single core peptide from polyacrylamide gels to nitrocellulose sheets (Western blotting), which reacted with anti-HBeAg/1 and anti-HBeAg/2. Selective discrimination of the two HBe antigens was achieved by radioimmunoassay (RIA). When highly purified core particles were incubated at 37°C in a 0.1% SDS-0.1% 2-mercaptoethanol solution, only HBeAg/1 was released after 5 min incubation and the release of HBeAg/2 occurred only after prolonging incubation for 30 min. The course of degradation was also detected by CsCl density gradient centrifugation. These results indicate that HBeAg/1 is less closely associated with core particles than is HBeAg/2. Electron microscopy showed that the core particles from which HBeAg/1 was removed were more labile than the original preparation when incubated at 56 °C in aqueous solution, or at 37 °C in Sarkosyl solutions; when placed in 1 -NaCl or -CsCl solution, the particles swelled to a larger diameter than untreated cores.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-65-2-405
1984-02-01
2019-11-18
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-65-2-405
Loading

Most Cited This Month

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error