The preparation and physicochemical characterization of an injectable form of reconstituted, glutaraldehyde cross-linked, bovine corium collagen.
Pepsin-solubilized bovine corium collagen was purified, reconstituted, and treated with various levels of glutaraldehyde. Treatment of suspensions of fibrillar collagen with low concentrations of glutaraldehyde appeared to have little effect on the gross morphology of fibrils, as judged by electron microscopy, but did have a significant impact on their physicochemical stability. Fibrillar collagen treated with glutaraldehyde at a concentration equal to or greater than 0.0075% demonstrated significant decreases in neutral solubility at elevated temperatures as compared to noncross-linked controls. Differential scanning calorimetry provided a convenient and quantitative means to correlate increases in melting temperature with increases in glutaraldehyde treatment concentration. Fibrillar collagen cross-linked with glutaraldehyde concentrations as low as 0.0075% demonstrated a significantly greater resistance to proteolytic degradation than did noncross-linked fibrillar collagen samples. The residual, extractable aldehyde content of such preparations was between 1 and 3 ppm. Rheological measurements on such cross-linked suspensions demonstrated that they were non-Newtonian, shear-thinning fluids, and that they were two- to threefold more viscous than corresponding preparations of noncross-linked collagen.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001705:Bioprosthesis; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003094:Collagen; D004591:Electrophoresis, Polyacrylamide Gel; D008854:Microscopy, Electron; D010447:Peptide Hydrolases / Q000032:analysis; D019736:Prostheses and Implants; D014783:Viscosity
D000596:Amino Acids; D003094:Collagen; D010447:Peptide Hydrolases