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Abstract

A process is described to purify collagen fibers while allowing the individual constituent molecules to retain their native configuration and 3-dimensional arrangement characteristic of the tissues from which they are derived. Collagenous tissues used as sources of purified collagen and for manufacturing bioprosthesis contain significant amounts of other substances (elastin, glycoproteins, polysaccharides, cell derived materials, etc.). This process becomes therefore useful to selectively preserve the collagen in its native conformation and to eliminate contaminants. The method described allows for enzymatic removal of all extraneous materials while preserving the native collagen molecules in their original fiber configuration. Subsequently this network of native collagen fibrils can be crosslinked using standard bifunctional crosslinking reagents, treated with other chemical substances, physical methods of insolubilization, or can be disrupted chemically or mechanically into smaller molecular aggregates or into the constituent single molecules.

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First Claim