Collagenase and neutral metallo-proteinase activity in extracts of inflamed human gingiva.

Collagenase and neutral metallo-proteinase activity in extracts of inflamed human gingiva.
复制标题

发炎的人牙龈提取物中的胶原酶和中性金属蛋白酶活性。

DOI:
10.1111/j.1600-0765.1981.tb00992.x
复制
发表时间:
1981
影响因子:
3.5
通讯作者:
Robinson,PJ
Robinson,PJ
中科院分区:
医学3区
文献类型:
--
作者:
Uitto,VJ;Appelgren,R;Robinson,PJ

文献摘要

被引文献

相似文献

发现人类牙龈含有中性蛋白水解酶,可降解天然和变性胶原蛋白,以及azocoll,一种非特异性蛋白酶的底物。当在0.1 M CaCl2存在下在40°C下提取不溶性牙龈匀浆时,获得最佳酶回收率。蛋白酶主要以潜在形式存在于提取物中,可被与蛋白质巯基反应的化合物激活。酶抑制剂研究表明,这三种酶都属于金属蛋白酶。在凝胶过滤层析中,降解变性胶原的酶活性与另外两种蛋白酶活性分离。当将特异性胶原酶活性和非特异性蛋白酶活性与牙龈指数进行比较时,发现显示明显炎症迹象的牙龈样本中的酶活性显着高于临床非炎症样本。
Human gingiva was found to contain neutral proteolytic enzymes that degrade native and denatured collagen, and azocoll, a substrate for non‐specific proteinases. The best enzyme recovery was obtained when an insoluble gingival homogenate was extracted at 40°C in the presence of 0.1 M CaCl2. The proteinases were found to exist in the extracts mostly in a latent form that could be activated by compounds reacting with sulfhydryl groups of proteins. Enzyme inhibitor studies showed that all three enzymes belong to the group of metallo‐proteinases. In gel filtration chromatography the enzyme activity degrading denatured collagen was separated from the two other proteinase activities. When the specific collagenase activity and the nonspecific proteinase activity were compared with Gingival Index, it was found that the enzyme activities were significantly higher in gingival samples that showed clear signs of inflammation than in clinically non‐inflamed samples.