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Artigo Revisado por pares
BIBTEX RIS

Spectrophotometric assay for vertebrate collagenase

1985; Elsevier BV; Volume: 147; Issue: 2 Linguagem: Inglês

10.1016/0003-2697(85)90294-5

ISSN

1096-0309

Autores

Harold Weingarten, Joseph Feder,

Tópico(s)

Connective tissue disorders research

Resumo

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-OC2H5 as substrate in the presence of 4,4'-dithiodipyridine or Ellman's Reagent. A Km of 0.004 M and a kcat 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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