作者: C L Mainardi , C A Vater , E D Harris
DOI: 10.1016/S0021-9258(17)30180-1
关键词:
摘要: A potent inhibitor of human collagenases, released from tendon explants in culture, has been purified and partially characterized. The an estimated molecular weight 25,000. It is relatively heat-stable but undergoes loss activity following exposure to trypsin. inhibits trypsin-activated rheumatoid synovial collagenase as well the enzyme obtained polymorphonuclear leukocytes. No inhibition Clostridium histolyticum (clostridiopeptidase A, EC 3.4.24.3) was noted. This may be a factor regulation extracellular connective tissue catabolism.