[Identification of rabbit lens proteins by two-dimensional gel electrophoreses and mass spectrometry]

To study the role of lens proteomics using two-dimensional electrophoresis (2-DE) and mass spectrometry in order to exploring novel effective ways for cataract prevention and therapy.

The proteins of the three-month-year old rabbit lens were separated using immobilized pH gradients 2-DE. Image analysis was carried out using Image Master 2D Elite 3.01 software package. Most of the crystallines was identified by matrix assisted laser adsorption/ionization-time of-flight-mass spectrometry (MALDI-TOF-MS).

The maps of 2-DE showed that lens proteins were in the section of pH 5 - 9 and the relative molecular weight was 14,000 - 94,000, while relative molecular weight of more abundant crystalline was localized at 14,000 - 40,000. About 180 protein spots were detected with the similar PI, molecular weight and quantity of each spot could be acquired by image analysis software. Sixteen crystallines were identified using MALDI-TOF-MS.

Proteomic analysis of lens can be accomplished and the proteins can be well separated and analyzed using 2-DE and mass spectrometry. This technique offers a new avenue for analyses of lens proteins and to assess their differential expression in cataract, and may thus provide a novel approach to cataract prevention and therapy.