The glutathionylation of human lens proteins was examined by Western-blot analysis with an anti-GSH antibody and scanning. Several different glutathionylated proteins were observed, and a 47 kDa band was of particular interest. This band did not appear after SDS/PAGE under reducing conditions, suggesting that it was a glutathionylated fraction. The 47 kDa band was found principally in the outer part of the lens, the cortex, but not in the lens nucleus where older proteins are present. The 47 kDa component was composed of βB1-, βB2- and γS-crystallin, with the γS-crystallin having glutathione bound at Cys-82 and at Cys-22, Cys-24 or Cys-26. We conclude that when glutathione becomes bound to γS-crystallin, it causes it to bind in turn to the β-crystallin polypeptides to form a dimer.
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Research Article|
May 01 2004
The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens
Jane CRAGHILL;
Jane CRAGHILL
*Nuffield Laboratory of Ophthalmology, University of Oxford, Walton Street, Oxford OX2 6AW, U.K.
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Andrew D. CRONSHAW;
Andrew D. CRONSHAW
†Structural Biochemistry Group, University of Edinburgh, Michael Swann Building, King's Buildings, Mayfield Road, Edinburgh EH9 3JR, Scotland, U.K.
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John J. HARDING
John J. HARDING
1
*Nuffield Laboratory of Ophthalmology, University of Oxford, Walton Street, Oxford OX2 6AW, U.K.
1To whom correspondence should be addressed (e-mail john.harding@eye.ox.ac.uk).
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Publisher: Portland Press Ltd
Received:
September 08 2003
Revision Received:
January 26 2004
Accepted:
February 05 2004
Accepted Manuscript online:
February 05 2004
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London ©2004
2004
Biochem J (2004) 379 (3): 595–600.
Article history
Received:
September 08 2003
Revision Received:
January 26 2004
Accepted:
February 05 2004
Accepted Manuscript online:
February 05 2004
Citation
Jane CRAGHILL, Andrew D. CRONSHAW, John J. HARDING; The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens. Biochem J 1 May 2004; 379 (3): 595–600. doi: https://doi.org/10.1042/bj20031367
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