碩士 / 國立臺灣大學 / 生化科學研究所 / 93 / The lens of the eye, which is crucial for light focusing, is the only transparent tissue in the vertebrate body. Crystallins are the major structural proteins of the eye lens that are responsible for its light refractive power. The crystallins make up more than 90% of the total dry mass of the lens. In vertebrates, there are in general, three classes of ubiquitous crystallins, i.e. alpha-, beta-, and gamma-crystallins. alpha-Crystallin, a member of small heat shock protein family, plays an important role as a molecular chaperone to prevent thermo-, chemical-, and UV- induced protein aggregation. In this thesis, we analyzed the global protein profiles of pig and catfish lenses by using high-resolution two-dimensional gel electrophoresis (2-DE) combined with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-Mass). Protein spots were identified by bioinformatics databases search and peptide mass comparison. The results revealed the common presence of alpha-, beta-, and gamma-crystallins in three evolutionarily distant species. Distinct differences in charge heterogeneity and molecular size of various crystallins can be found between these two species.
| Identifer | oai:union.ndltd.org:TW/093NTU05103005 |
| Date | January 2005 |
| Creators | Cheng-Hung Wu, 吳承鴻 |
| Contributors | 邱式鴻 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 66 |
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