Wize J, Knäuper V, Tschesche H
Department of Biochemistry, Institute of Rheumatology, Warszawa, Poland.
Acta Biochim Pol. 1990;37(1):201-6.
Latent collagenase has been isolated in pure form from the rheumatoid synovial fluid. The final preparation, activated by trypsin, yielded a collagenase of specific activity 2,227 units/mg. Electrophoresis in sodium dodecyl sulfate polyacrylamide gels revealed a protein doublet of 54 and 50 kDa. Trypsin or HgCl2 activation resulted in disappearance of the doublet and emergence of a new doublet of 47 and 43 kDa. The latent collagenase could also be activated by leucocyte cathepsin G or plasmin. Neither the latent nor the active collagenase from synovial fluid showed any cross-reactivity with the antibodies against leucocyte collagenase. The trypsin activated collagenase degraded collagen type I, II, III giving typical cleavage products but did not degrade type IV and V collagen.
已从类风湿性滑液中以纯形式分离出潜伏胶原酶。经胰蛋白酶激活的最终制剂产生了比活性为2227单位/毫克的胶原酶。在十二烷基硫酸钠聚丙烯酰胺凝胶中进行电泳显示出54和50 kDa的蛋白质双峰。胰蛋白酶或HgCl₂激活导致双峰消失，并出现47和43 kDa的新双峰。潜伏胶原酶也可被白细胞组织蛋白酶G或纤溶酶激活。来自滑液的潜伏胶原酶和活性胶原酶与抗白细胞胶原酶的抗体均未显示任何交叉反应。胰蛋白酶激活的胶原酶可降解I型、II型、III型胶原，产生典型的裂解产物，但不能降解IV型和V型胶原。
