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Spectrophotometric assay for vertebrate collagenase

Authors
Journal
Analytical Biochemistry
0003-2697
Publisher
Elsevier
Publication Date
Volume
147
Issue
2
Identifiers
DOI: 10.1016/0003-2697(85)90294-5
Keywords
  • Enzyme Assay
  • Vertebrate Collagenase
  • Esterase
  • Substrate
Disciplines
  • Biology

Abstract

Abstract Collagenase from normal human skin fibroblasts was found to catalyze the hydrolysis of esters and thio esters. This observation led to the development of a rapid, sensitive, continuous spectrophotometric assay for vertebrate collagenase using the thio peptolide Ac-ProLeuGly- S-LeuLeuGly-OC 2H 5 as substrate in the presence of 4,4′-dithiodipyridine or Ellman's Reagent. A K m of 0.004 m and a k cat of 370,000 h −1 were determined for the thio peptolide-enzyme reaction. The method is able to detect collagenase at concentrations as low as 2 ng/ml.

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