Pseudo-zero order solubilization of remazol-brilliant-blue elastin by elastase
✍ Scribed by Joseph Bieth; Monique Pichoir; Pierre Metais
- Publisher
- Elsevier Science
- Year
- 1976
- Tongue
- English
- Weight
- 208 KB
- Volume
- 70
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
Conditions are described under which linear responses of optical density to time and enzyme concentration are experienced in the course of the elastase-catalyzed solubilization of remazol-brilliant-blue elastin.
According to Gertler (1), elastase may be defined as a proteolytic enzyme which is able to adsorb on insoluble elastin and whose side chain specificity is directed toward nonpolar aliphatic amino-acid residues. Elastin substrates must thus be used together with model substrates (2,3) in order to characterize unambiguously a new enzyme as "an elastase."
In 1968, Rinderknecht et al. (4) used elastin covalently labelled with remazol-brilliant-blue as a new elastase substrate, which had the outstanding advantage over noncovalently labelled congored or orcein elastins not to be subject to delabelling by nonenzymic proteins. However, a serious'drawback of the method described by Rinderknecht et al. (4) is that it yields curvilinear responses of optical density to time and enzyme concentration (4,5,6), as do most assays using natural elastase substrates (8). In this paper, we describe conditions under which the enzymic solubilization of remazol-brilliant-blue elastin is pseudo-zero order.