Abstract Preliminary characterization of the human enamel matrix at 16–18 weeks in utero was performed. Using an homogenizing buffer, the proteins were extracted and analysed by gel electrophoresis. Total cellular RNA was isolated and the cell-free mRNA translated. The major component was a 68,000 protein with an enamelin-like amino-acid composition. Other translation products included a 55,000 polypeptide and lower mol. wt components of 26,000, 22,000 and 20,000 size of amelogenin size. It is suggested that high mol. wt component in the enamelin range is the most prevalent at the early stage of human tooth development.