Cleavage of native type I collagen by human neutrophil elastase

摘要: The ability of purified human neutrophil elastase (EC 3.4.21.37) to cleave native type I collagen has been investigated. Soluble human, bovine or rat was incubated with for 16 h at 25 degrees C before catalysis stopped 3, 4-dichloroisocoumarin. Analysis by SDS/PAGE the digests revealed 3/4-length fragments similar in size those produced interstitial collagenase. collagenolytic activity dose dependent and not due a contaminating metalloproteinase cysteine proteinase, as it inhibited 1,10-phenanthroline, EDTA L-trans-epoxysuccinyl-leucylamido-(4-guanidino)butane. identity cleavage products confirmed using new antibody that recognizes unwound alpha2(I)-chain. This detected fragment following cleavage. In addition cleaving soluble collagen, also cleaved reconstituted, radiolabelled fibrils, rate microg/min per nmol. These results indicate can helix, an might contribute its roles connective-tissue pathology.