Abstract
Two basic histodine-rich proteins were isolated from human submandibularsublingual saliva by means of hydroxyapatite chromatography and CM-cellulose chromatography. These two proteins were characterized by a high content of basic amino acids such as Lys, Arg, and His in their amino acid composition and had a strong affinity with hydroxyapatite crystals.
These two proteins had molecular weights of 9,000 and 6,000 daltons respectively, but they had the same N-terminal amino acid sequence up to 20 residues. The fraction of hydroxyapatite chromatography, which contained mainly these two basic histidine-rich proteins, accelerated the hydroxyapatite crystal growth in the solution saturated with dicalcium phosphate salt. Based on these results, it is considered that they might play some role in formation of the acquired pellicle and dental calculus. The concentration of these basicproteins in parotid saliva had no correlation to the DMFT index examined in 28 cases of adults females.
