## Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates and identification of protein spots by microsequencing Employing isoelectric focusing on immobilized pH gradients followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) we have obtained a map of
Analysis of the proteins of aging Caenorhabditis elegans by high resolution two-dimensional gel electrophoresis
β Scribed by Dr. Jacques R. Vanfleteren; Annemie De Vreese
- Publisher
- John Wiley and Sons
- Year
- 1994
- Tongue
- English
- Weight
- 864 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0173-0835
No coin nor oath required. For personal study only.
β¦ Synopsis
The metabolic rate decreases dramatically as a function of age in the nematode worm Caenorhabditis elegans. Superoxide anion production, which is tightly linked to oxygen consumption, and thus to metabolic rate, drops to a 20-fold lower level in 10-day-old, senescent worms, as compared to 4-day-old young adults. In a long-lived mutant strain of the same species metabolic activity is much better preserved. High resolution two-dimensional gel electrophoresis was employed to study alterations in the protein profile, correlating with changes of metabolic activity. Surprisingly, few proteins show age-or ageand strain-specific variations of spot intensity. The abundance of the huge majority of proteins displayed on these gels remains unaltered, irrespective of age and strain differences. These results imply that there are no major agerelated alterations of proteins due to faulty protein synthesis or free radical attack, and that age-related changes in the rate of protein synthesis and breakdown must be strictly coordinated throughout the aging process.
Materials and methods
2.1 Strains, culture methods and age cohorts
C. elegans strains TJ412 and BA713 were obtained from
π SIMILAR VOLUMES
## Abstract In order to further the understanding of proteinβsurface interactions in the coagulation system, we have chosen to study plasma protein adsorption onto heparin immobilized surfaces. Heparinβbinding proteins are abundant in plasma: a search of amino acid sequences revealed that many plas