TY - JOUR
T1 - Assignment of disulfide bonds in the X protein (HBx) of hepatitis B virus
AU - Gupta, Aparna
AU - Mal, Tapas
AU - Jayasuryan, N.
AU - Chauhan, Virander S.
PY - 1995/7/26
Y1 - 1995/7/26
N2 - We have established the disulphide arrangement of cysteines in E. coli expressed HBx by chromatographic analysis of enzymatically cleaved protein and sequence analysis of cysteine containing fragments. Eight of the nine cysteines are disulphide linked in an interesting pattern. Each cysteine is linked to the fourth cysteine in a sequential manner and the last cysteine is free; the disulphide linkages are between Cys7 and Cys78, CyS17 and Cys115, Cys61 and Cys137, Cys69 and Cys143 while Cys148 is free.
AB - We have established the disulphide arrangement of cysteines in E. coli expressed HBx by chromatographic analysis of enzymatically cleaved protein and sequence analysis of cysteine containing fragments. Eight of the nine cysteines are disulphide linked in an interesting pattern. Each cysteine is linked to the fourth cysteine in a sequential manner and the last cysteine is free; the disulphide linkages are between Cys7 and Cys78, CyS17 and Cys115, Cys61 and Cys137, Cys69 and Cys143 while Cys148 is free.
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U2 - 10.1006/bbrc.1995.2057
DO - 10.1006/bbrc.1995.2057
M3 - Article
C2 - 7626131
AN - SCOPUS:0029087168
SN - 0006-291X
VL - 212
SP - 919
EP - 924
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -
