Abstract
Insoluble collagen from bovine bone was digested with pepsin at 25°C in 0.01 N HCI. About 97% of the material was solubilized by repeated digestion for 24 hr each. From this pepsin digested bone collagen, segment-long-spacing (SLS) aggregate as well as native types of reconstituted fiber was obtained. Both types of the aggregate were convertible into each other by solubilization and reconstitution. Characterization of the solubilized bone collagen by disc electrophoresis and observation of the aggregates with an electron microscope are reported. Significance of the findings was discussed from the point of the tissue specific property of bone collagen. This is the first demonstration of the solubilization of insoluble bone collagen with protease and its reconstitution as the SLS aggregate.
