Digitale Medien
Oxford, UK
:
Blackwell Publishing Ltd
Journal of periodontal research
16 (1981), S. 0
ISSN:
1600-0765
Quelle:
Blackwell Publishing Journal Backfiles 1879-2005
Thema:
Medizin
Notizen:
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.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1111/j.1600-0765.1981.tb00992.x
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