Interaction between alpha and upsilon‐crystallin, common to the eye of the Australian platypus, by radical probe mass spectrometry

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Abstract
The interaction between α‐crystallin and υ‐crystallin, a class recently discovered in the eye of the Australian platypus, has been shown by native shift gel assay and examined by radical probe mass spectrometry in the context of the ability of α‐crystallin to protect υ‐crystallin from oxidation and oxidative damage through radical‐based oxidative stress mechanisms. Residues 22–41, 132–148, 212–227 and 245–264 of υ‐crystallin display the greatest protection when interacted with α‐crystallin at a ratio of 2 : 1 observed for the complex, which is commensurate with their levels measured in the eye of the platypus. Across each domain, a delay in the onset of oxidative damage is observed as the time of exposure to radicals is increased. The results are discussed in the context of the structure of the porcine homologue of υ‐crystallin. Copyright © 2006 John Wiley & Sons, Ltd.