Monoclonal antibodies to different epitopes in amelogenins from fetal bovine teeth recognize high-molecular-weight components.

Enamel proteins were extracted and partitioned into amelogenin and enamelin fractions. Although several attempts were made to raise monoclonal antibodies to each protein fraction, monoclonal antibodies were only obtained against the amelogenin fraction. Six monoclonal antibodies were generated, and these could be classified into three groups recognizing different epitopes by a competitive enzyme-linked immuno-absorbent assay. A model for the arrangement of the epitopes is proposed. In Western-blotting experiments, all six monoclonal antibodies recognized amelogenin components of approx. 45,000 and 60,000 daltons as well as lower molecular-weight components of 10,000 to 30,000. It is proposed that the 45,000 and 60,000 dalton components are precursors of the lower molecular-weight components.