Enamel proteins are extracellular matrix proteins expressed throughout enamel formation. However, questions concerning their numbers and origins are still somewhat ambiguous. To characterize the nascent enamel proteins, cell free translation and immunoprecipitation procedures were performed using poly(A)$ sp{+}$RNA isolated from freeze-dried segments of rat incisor enamel organs at the secretory, early maturation, and mid maturation stages of amelogenesis. Phosphoimaging revealed that the enamel organ produces enamel proteins continuously throughout enamel development albeit in decreasing number and intensity. Ten enamel proteins were translated at the secretory stage and ranged in molecular weight from 80 to 18 kDa, resembling the number (Simmer et al., 1994) and the size (DenBesten et al., 1992) of RNA transcripts recently described for murine and rat. At the early and mid maturation stages, the enamel proteins span a 27 to 68 kDa region. This selected expression of enamel proteins at each stage of development suggests that specific proteins may be important for the maturation process.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.22851 |
| Date | January 1995 |
| Creators | Braganza, Annabel M. H. (Mary Helen) |
| Contributors | Smith, Charles (advisor) |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Master of Science (Department of Anatomy and Cell Biology.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 001467625, proquestno: MM08000, Theses scanned by UMI/ProQuest. |
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