1. Post-translational modification of betaH-crystallin of bovine lens with aging.
- Author
-
Kamei A, Takeuchi N, Nagai M, and Mori S
- Subjects
- Acetylation, Animals, California, Cattle, Chromatography, Gel methods, Chromatography, Ion Exchange methods, Crystallins chemistry, Crystallins isolation & purification, Crystallins metabolism, Databases, Protein, Electrophoresis, Gel, Two-Dimensional methods, Phosphorylation, San Francisco, Sequence Analysis, Protein, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization methods, Trypsin metabolism, Aging, Lens, Crystalline chemistry, Lens, Crystalline metabolism, Protein Processing, Post-Translational
- Abstract
This study investigates post-translational modification of proteins of bovine lens with aging (3 year old vs. 6 month old cows). After water-soluble proteins were submitted to gel and ion exchange chromatography, betaH-crystallin, a subunit of beta-crystallin, and modified materials were isolated. These materials were then submitted to two dimensional polyacrylamide gel electrophoresis (2D-SDS PAGE) to detect and isolate the new spots. Results for lens proteins from 3 year old animals were compared to those from 6 month old animals. All spots were digested in gel with trypsin and the molecular masses of tryptic digests were measured by matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOFMS). Peptides peaks obtained from mass mapping were identified using the protein database of the MS-Fit program in the Protein prospector program of the University of California, San Francisco. We found that two post translational modifications of betaH-crystallin, acetylation and phosphorylation occurred with aging.
- Published
- 2003
- Full Text
- View/download PDF