Abstract
Proteoglycans in a smaller size present in the bone and dentin are considered to play some role in the differentiation and calcification. The purpose of this study is to characterize the biochemical and immunological properties of the bone and dentin proteoglycans, especially their core proteins.
The proteoglycans were extracted with EDTA/guanidine HCl from the bovine bone and dentin and purified by the DEAE-Sephacel and Sepharose CL-6B chromatography. The purified proteoglycans were digested with chondroitinase ABC and the core proteins from the dentin proteoglycan were used to raise the monoclonal antibody.
Both the bone and dentin proteoglycans were found to contain glycosaminoglycan and protein in equal amounts. The core proteins of the bone proteoglycan were shown to consist of 45 K, 40 K and 35K in molecular weight, whereas those of the dentin were 90K, 70K, 40K and smaller. The proteoglycan core proteins of 40 K and smaller sizes in the dentin were immunologically similar not only to those of the bone but also to those of the cartilage, tendon and dental pulp.
