Abstract: A truncated mutant of the 92 kDa gelatinase is disclosed which is catalytically active comparable to the full-length enzyme but, unlike the full-length enzyme, is essentially inactive against insoluble elastin. The truncated mutant preferably comprises residues 107-217 fused to residues 391-443 of the parent molecule. The truncated mutant is useful for treatment of disorders requiring the removal of excess connective tissue.

Abstract: A truncated mutant of the 92 kDa gelatinase is disclosed which is catalytically active comparable to the full-length enzyme but, unlike the full-length enzyme, is essentially inactive against insoluble elastin. The truncated mutant preferably comprises residues 107-217 fused to residues 391-443 of the parent molecule. The truncated mutant is useful for treatment of disorders requiring the removal of excess connective tissue.

Abstract: A method of stimulating chemotaxis toward a prosthetic device is disclosed, which method comprises incorporating a chemotactic peptide of the formulaB.sup.1 -X-(APGVGV).sub.n -Y-B.sup.2whereinA is a peptide-forming residue of L-alanine;P is a peptide-forming residue of L-proline;G is a peptide-forming residue of glycine;V is a peptide-forming residue of L-valine;B.sup.1 is H or a biocompatible N-terminal group;B.sup.2 is OH, OB.sup.3 where B.sup.3 is a non-toxic metal ion, or a biocompatible C-terminal group;X is PGVGV, GVGV, VGV, GV, V, or a covalent bond;Y is APGVG, APGV, APG, AP, A, or a covalent bond; andn is an integer from 1 to 100;into a surface of the prosthetic device. Prosthetic devices which have the property of enhancing invasion of elastic fiber synthesizing fibroblasts as a result of the chemotactic peptide are also disclosed.