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
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发表时间:
1981
影响因子:
3.5
通讯作者:
Robinson,PJ
中科院分区:
文献类型:
--
作者:
Uitto,VJ;Appelgren,R;Robinson,PJ
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.