Injectable cross-linked collagen with improved flow properties.

Aqueous suspensions of glutaraldehyde cross-linked fibrillar collagen and non-cross-linked fibrillar collagen were examined by rheometry, particle size analysis, and microscopic techniques. Although cross-linked collagen suspensions were similar to non-cross-linked suspensions by microscopic and size analyses, they differed in rheometric properties. Concentric cylinder Couette flow, shear creep, uniaxial creep, and porous bed flow all revealed that cross-linked collagen was more resistant to deformation and flow than non-cross-linked collagen.

Proteoglycans from bovine fetal epiphyseal cartilage. Sedimentation velocity and light scattering studies of the effect of link protein on proteoglycan aggregate size and stability.

Proteoglycan monomer and link proteins were isolated from bovine fetal epiphyseal cartilage and characterized. The physical characteristics of proteoglycan monomer were: s0(20) = 21.3 S, D0t,z = 4.

Thermal and solvent stability of proteoglycan aggregates by quasielastic laser light-scattering.

The dissociation behavior of several species of proteoglycan aggregates (PGA) has been studied quantitatively by monitoring the changes in particle size by dynamic laser light-scattering. Firstly, studies of the thermal dissociation of reconstituted PGA from bovine nasal septum and bovine fetal epiphysus are described. The effect of link protein in stabilizing reconstituted PGA against changes in temperature has been demonstrated.

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.