Abstract
Amelogenin enamel-protein epitopes in developing incisors were ultrastructurally localized with high specificity resolution. They formed clumps scattered over the enamel organic matrix between the hydroxyapatite crystals, and were also present over islands of stippled or granular material at the forming surface of the enamel matrix demonstrating that this material consists in part of amelogenin enamel protein. The amounts of amelogenin, as judged by labelling density, were not greater in the stippled or the surface crystal-containing matrix as compared to the enamel matrix up to 50 μm deep. Amelogenins were also localized in the rough endoplasmic reticulum, Golgi apparatus and secretory granules of the ameloblasts, which suggests they are merocrine secretions.
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