PUB - Publikationen an der Universität Bielefeld

Human polymorphonuclear-leucocyte collagenase (M(r) 64000) shows autoproteolytic degradation to two major fragments of M(r) 40000 and M(r) 27000. N-terminal sequence data and investigation of the substrate specificity of the fragments demonstrate that the M(r)-40 000 fragment corresponds to the catalytic domain, whereas the M(r)-27000 fragment shows no enzymic activity. The activity profile of the M(r)-40000 fragment is comparable with the specificity of the intact active collagenase (M(r) 64000), but the ability to cleave collagen was lost. The enzymic activity of this fragment can be inhibited by either tissue inhibitor of metallo-proteinase (TIMP)-1 or recombinant TIMP-2 in a 1:1 molar ratio. The C-terminal part of the enzyme (M(r) 27000), important for the binding reaction with collagen substrates, is involved in collagenolysis.