Interaction between alpha and upsilon-crystallin, common to the eye of the Australian platypus, by radical probe mass spectrometry.
The interaction between alpha-crystallin and upsilon-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 alpha-crystallin to protect upsilon-crystallin from oxidation and oxidative damage through radical-based oxidative stress mechanisms. Residues 22-41, 132-148, 212-227 and 245-264 of upsilon-crystallin display the greatest protection when interacted with alpha-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 upsilon-crystallin.
Issa
Samah
S
School of Molecular & Microbial Biosciences, University of Sydney, Australia.
Downard
Kevin M
KM
D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003459:Crystallins / Q000737:chemistry*; D005123:Eye / Q000737:chemistry*; D005136:Eye Proteins / Q000737:chemistry; D006868:Hydrolysis; D007202:Indicators and Reagents; D013058:Mass Spectrometry; D008968:Molecular Conformation; D010084:Oxidation-Reduction; D010987:Platypus / Q000378:metabolism*; D014357:Trypsin; D038201:alpha-Crystallins / Q000737:chemistry*
D003459:Crystallins; D005136:Eye Proteins; D007202:Indicators and Reagents; D038201:alpha-Crystallins; D014357:Trypsin