The enameloid matrix consists of a collagenous matrix, and non collagenous proteins. Mature enameloid is highly mineralised similarly to mammalian enamel a large amount of the protein being removed. This is in contrast with bone, cementum, and dentin, where a large amount of collagen remains in the completed tissue. From the results of a biochemical study it has been suggested that the decrease of a major part of both the collagenous protein in developing enameloid is brought about by proteolytic enzymes (Kawasaki et al. 1987). However, histological and histochemical observations were not made at that time. In this study fourty-five live specimens of Sea Bream (Pagrus major) were used for histological and histochemical observations. Four undemineralised serial cryostat sections were obtained from each tooth garm and the developing enameloid matrix was observed ultrastructurally. The results of this study, show that the proteolytic enzyme activity which could not be detected in the enameloid formative stage, but was demonstrable after mineralisation had spread across the thickness of the matrix. Further more, the stage at which the proteolytic enzyme could be obtained was related to the stage of ALPase activity found in the dental epithelial cells.