Proteoglycan-degrading enzymes of rabbit fibroblasts and granulocytes.

摘要: A neutral proteinase secreted by rabbit synovial fibroblasts in parallel with specific collagenase was partially purified ion-exchange chromatography. At pH 7.6 this degraded 35S-labelled bovine nasal proteoglycan and azo-casein. The enzymic activity inhibited EDTA, 1,10-phenanthroline serum, whereas di-isopropyl phosphorofluoridate soya-bean trypsin inhibitor had little effect. By gel filtration the apparent mol.wt. of enzyme 25000. fibroblast compared proteoglycan-degrading proteinases polymorphonuclear-leucocyte granules. Two distinct activities were found granules: one other EDTA. polymorphonuclear leucocytes at acid also examined. Both cathepsin D a thiol-dependent contributed to degradation 4.5.