Heterogeneity among the odontoblast-specific, highly phosphorylated acidic protein dentine phosphoprotein (DPP) obtained from different species has been reported by several investigators. In the present study, the apparent molecular-mass variations in rabbit and mouse DPP were investigated. Extracellular matrix (ECM) DPPs were isolated and characterized. Primary gene products, before post-translational phosphorylation, were analysed based upon translation products produced in a rabbit reticulocyte lysate cell-free system using a polyclonal mouse anti-DPP antibody. Nascent non-phosphorylated DPPs were also identified from intracellular protein extracts. Mouse and rabbit ECM phosphoproteins exhibited a 10 kDa difference in size. However, nascent intracellular or translation products from both species showed the same lower molecular mass (approx. 45 kDa). Furthermore, Northern-blot analysis showed a single mRNA of the same size in both species (approx. 1.6 kb) which contains information for a protein no larger than 50 kDa. Our results indicate that the difference in molecular mass (or electrophoretic behaviour) among DPPs from different species is due to post-translational modifications, in this case phosphorylation.