Lazarus G S, Daniels J R, Brown R S, Bladen H A, Fullmer H M
J Clin Invest. 1968 Dec;47(12):2622-9. doi: 10.1172/JCI105945.
This report suggests a mechanism for collagen degradation mediated by human granulocytic leukocytes. A specific collagenase, which is extractable from human granulocytes, has been partially purified by DEAE chromatography. This collagenolytic enzyme is operative at physiological pH and is inhibited by EDTA, cysteine, and reduced glutathione but not by human serum. The enzyme cleaves the collagen molecule into two specific products, without loss of helical conformation. Electron micrographs of segment long spacing aggregates indicate that the cleavage occurs one-quarter of the length from the carboxy terminal end of the molecule. Experiments with crude extracts from granulocytes suggest that the specific products of granulocyte collagenase activity are then degraded by other proteases present in the human granulocyte.
本报告提出了一种由人类粒细胞介导的胶原蛋白降解机制。一种可从人类粒细胞中提取的特异性胶原酶已通过DEAE柱层析进行了部分纯化。这种胶原olytic酶在生理pH值下具有活性，并且受到EDTA、半胱氨酸和还原型谷胱甘肽的抑制，但不受人血清的抑制。该酶将胶原蛋白分子切割成两种特定产物，而不会丧失螺旋构象。片段长间距聚集体的电子显微镜照片表明，切割发生在分子羧基末端长度的四分之一处。对粒细胞粗提物的实验表明，粒细胞胶原酶活性的特定产物随后会被人类粒细胞中存在的其他蛋白酶降解。
