ASSIGNMENT OF DISULFIDE BONDS IN THE X-PROTEIN (HBX) OF HEPATITIS-B VIRUS

Authors
GUPTA A MAL TK JAYASURYAN N CHAUHAN VS
Citation
A. Gupta et al., ASSIGNMENT OF DISULFIDE BONDS IN THE X-PROTEIN (HBX) OF HEPATITIS-B VIRUS, Biochemical and biophysical research communications, 212(3), 1995, pp. 919-924
Citations number
8
Categorie Soggetti
Biology,Biophysics
Journal title
Biochemical and biophysical research communications → ACNP
ISSN journal
0006291X
Volume
212
Issue
3
Year of publication
1995
Pages
919 - 924
Database
ISI
SICI code
0006-291X(1995)212:3<919:AODBIT>2.0.ZU;2-V
Abstract
We have established the disulphide arrangement of cysteines in E. coli expressed HBx by chromatographic analysis of enzymatically cleaved pr otein and sequence analysis of cysteine containing fragments. Eight of the nine cysteines are disulphide linked in an interesting pattern. E ach cysteine is linked to the fourth cysteine in a sequential manner a nd the last cysteine is free; the disulphide linkages are between Cys( 7) and Cys(78), CyS(17) and CyS(115), Cys(61) and Cys(137), Cys(69) an d CyS(143) while Cys(148) is free. (C) 1995 Academic Press, Inc.