Changes in the protein components of rat incisor enamel during tooth development

Enamel-matrix components from rat incisor enamel were extracted from tissue at different stages of development on single teeth. Separations of proteins using urea and SDS acrylamide gel electrophoresis were compared. The bulk of the matrix exhibited SDS mol. wt of 25-30,000 with smaller amounts at approximately 18,000 and about 10-12,000. Trace amounts of material at -50,000 and 70,000 were detected. These were presumably associated with the mineral phase as their yield increased after demineralization. The proportion of small molecular weight components increased with tissue age. Using urea, many more proteins were separated (up to 20) into fast, intermediate and slowly-migrating components. Disappearance of small bands of intermediate mobility at the end of matrix secretion suggested that they were early ameloblast products which were rapidly degraded after secretion. Both slowly- and rapidly-migrating components increased with tissue age indicating progressive degradation of parent molecules of intermediate mobility into highly charged and relatively uncharged molecules.