Collagenase in mineralized tissues of human teeth.
A collagenase cleaving native type I [14C]collagen but inactive against the synthetic substrate Pz-Pro-Leu-Gly-Pro-D-Arg was extracted from mineralized human dental tissue. The enzyme specifically degrades native collagen into characteristic products (3/4) and (1/4). Its apparent molecular mass of 68 kDa is relatively high in comparison with collagenases from other oral tissues. The enzyme is a metalloproteinase inhibited by low concentrations of the chelating agents EDTA, 1, 10-phenanthroline, alpha alpha'-dipyridyl, and not affected by diisopropylfluorophosphate, soybean trypsin inhibitor, and p-chloromercuribenzoate. It is stable to lyophilization and can be stored at-20 degrees C for at least 6 months.
Dumas
J
J
Hurion
N
N
Weill
R
R
Keil
B
B
D015082:2,2'-Dipyridyl / Q000494:pharmacology; D002852:Chromatography, Ion Exchange; D003094:Collagen / Q000378:metabolism; D003739:Dental Cementum / Q000201:enzymology*; D003743:Dental Enamel / Q000201:enzymology*; D003804:Dentin / Q000201:enzymology*; D004492:Edetic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D003012:Microbial Collagenase / Q000032:analysis*; D008970:Molecular Weight; D010618:Phenanthrolines / Q000494:pharmacology
D010618:Phenanthrolines; D015082:2,2'-Dipyridyl; D003094:Collagen; D004492:Edetic Acid; D003012:Microbial Collagenase; C025205:1,10-phenanthroline