The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens

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, sugge...

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Veröffentlicht in:	Biochemical journal 2004-05, Vol.379 (Pt 3), p.595-600
Hauptverfasser:	Craghill, Jane, Cronshaw, Andrew D, Harding, John J
Format:	Artikel
Sprache:	eng
Schlagworte:	Aging - physiology Amino Acid Sequence Blotting, Western Cataract - metabolism Cysteine - genetics Cysteine - metabolism Dimerization Disulfides - chemistry Disulfides - metabolism Electrophoresis, Polyacrylamide Gel gamma-Crystallins - chemistry gamma-Crystallins - metabolism Glutathione - chemistry Glutathione - metabolism Humans Lens, Crystalline - chemistry Molecular Sequence Data Molecular Weight
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