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Collagenase in mineralized tissues of human teeth
Author(s) -
Dumas J.,
Hurion N.,
Weill R.,
Keil B.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81212-6
Subject(s) - collagenase , chemistry , trypsin , enzyme , chelation , biochemistry , molecular mass , substrate (aquarium) , mineralized tissues , metalloproteinase , microbiology and biotechnology , dentin , biology , dentistry , medicine , ecology , organic chemistry
A collagenase cleaving native type I [ 14 C]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 ( ) and ( ). 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, αα'‐dipyridyl, and not affected by diisopropylfluorophosphate, soybean trypsin inhibitor, and p ‐chloromercuribenzoate. It is stable to lyophilization and can be stored at −20°C for at least 6 months.