Gibson W T, Milsom D W, Steven F S, Lowe J S
Biochem J. 1978 Apr 15;172(1):83-9. doi: 10.1042/bj1720083.
Collagenolytic cathepsin activity was detected in lysed rabbit peritoneal polymorphonuclear leucocytes. The pH optimum was around 3, and activity was greatly enhanced by the presence of cysteine and EDTA. Digestion of polymeric collagen resulted in the release of alpha, beta, and gamma-chains. Collagenolytic cathepsin activity was associated mainly with the granule fraction isolated from homogenates by differential centrifugation. The granule fraction was further fractionated by isopycnic density-gradient centrifugation, and the collagenolytic cathepsin activity was shown to be associated with the azurophil and tertiary granules, both lysosome-like organelles.
在裂解的兔腹膜多形核白细胞中检测到胶原olytic组织蛋白酶活性。最适pH约为3，半胱氨酸和乙二胺四乙酸（EDTA）的存在极大地增强了活性。聚合胶原的消化导致α、β和γ链的释放。胶原olytic组织蛋白酶活性主要与通过差速离心从匀浆中分离出的颗粒部分相关。通过等密度密度梯度离心对颗粒部分进一步分级分离，结果表明胶原olytic组织蛋白酶活性与嗜苯胺蓝颗粒和三级颗粒相关，这两种颗粒都是类似溶酶体的细胞器。
