Assignment of disulfide bonds in the X protein (HBx) of hepatitis B virus

Aparna Gupta; Tapas Mal; N. Jayasuryan; Virander S. Chauhan

doi:10.1006/bbrc.1995.2057

Assignment of disulfide bonds in the X protein (HBx) of hepatitis B virus

Aparna Gupta, Tapas Mal, N. Jayasuryan, Virander S. Chauhan

Chemistry

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24 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	919-924
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	212
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.1995.2057
State	Published - Jul 26 1995

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1006/bbrc.1995.2057

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abstract = "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.",

author = "Aparna Gupta and Tapas Mal and N. Jayasuryan and Chauhan, \{Virander S.\}",

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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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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Assignment of disulfide bonds in the X protein (HBx) of hepatitis B virus

Abstract

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