The Eye Lens Protein, γS Crystallin, Undergoes Glutathionylation-Induced Disulfide Bonding Between Cysteines 22 and 26

The Eye Lens Protein, γS Crystallin, Undergoes Glutathionylation-Induced Disulfide Bonding Between Cysteines 22 and 26

The oxidation of cysteines in crystallins is a major age-related modification associated with cataract formation. The purpose of this research was to determine the susceptibility of γS-crystallin to glutathionylation-induced oxidation and disulfide bond formation. Recombinantly expressed wild-type h...

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Bibliographic Details
Main Authors: Kate Halverson-Kolkind, David C. Thorn, Martin Tovar-Ramirez, Eugene Shakhnovich, Larry David, Kirsten Lampi
Format: Article
Language:English
Published: MDPI AG 2025-03-01
Series:Biomolecules
Subjects:
eye lens
crystallin
protein structure
glutathionylation
protein oxidation
mass spectrometry
Online Access:https://www.mdpi.com/2218-273X/15/3/402
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