Collagenase in mineralized tissues of human teeth.

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 Lett

journal_title

FEBS letters

authors

Dumas J,Hurion N,Weill R,Keil B

doi

10.1016/0014-5793(85)81212-6

subject

Has Abstract

pub_date

1985-07-22 00:00:00

pages

51-5

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(85)81212-6

journal_volume

187

pub_type

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