Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Dumas J,Hurion N,Weill R,Keil Bdoi
10.1016/0014-5793(85)81212-6subject
Has Abstractpub_date
1985-07-22 00:00:00pages
51-5issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(85)81212-6journal_volume
187pub_type
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