Abstract
Previously, an apatite-collagen complex was prepared by the incubation of phosvitin cross-linked collagen for one week in a daily renewed solution of calcium β-glycerophosphate in the presence of alkaline phosphatase.In the present study, such factors affecting precipitation of apatite on the collagen fibrils as solution concentration, amounts of alkaline phosphatase and phosvitin added, and the solution pH were investigated to obtain a better condition to synthe-size the apatite-rich-collagen complex.In solutions of β-glycerophosphate, the activity of alkaline phosphatase was examined over a range of pH values.The optimum pH for hydrolysis by alkaline phosphatase was around 10.0, slightly higher than the pH of the solution(8.50)previously used.Interestingly, phosvitin was found to increase the activity of alkaline phosphatase, resulting in more liberation of the inorganic phosphate.As a result, more apatite was precipitated on the collagen fibrils, although phosvitin has been known to be a strong inhibitor in the formation of apatite.
