Collagenase in the human periodontal ligament.
Collagenase activity was demonstrated by direct incubation to be present in human periodontal ligament. This activity was found in only one of two populations of ligament, i.e., those ligaments taken from teeth in which their attachment site was at least 2.5 mm apical to the cementoenamel junction. The collagenase was demonstrated to be of host origin because it degraded collagen into 3/4 and 1/4 alpha chain fragments characteristic of mammalian collagenases. The enzyme was shown to be inhibited in the presence of EDTA and to have a pH optimum of 7.5.
D003094:Collagen / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D006801:Humans; D003012:Microbial Collagenase / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000378:metabolism; D010510:Periodontal Diseases / Q000201:enzymology; D010513:Periodontal Ligament / Q000201:enzymology*; D012967:Sodium Dodecyl Sulfate; D014357:Trypsin / Q000494:pharmacology
D012967:Sodium Dodecyl Sulfate; D003094:Collagen; D014357:Trypsin; D003012:Microbial Collagenase