Abstract
We have detected protein photodegradation in the fluorescence unfolding kinetics experiment of stem bromelain, a cysteine proteinase from the papain family. Thermally induced unfolding has been followed by near and far circular dichroism and tryptophan fluorescence emission. It was found that the fluorescence kinetics involves two phases. This biphasic nature results from ultraviolet induced photolysis oftryptophan.
Protein & Peptide Letters
Title:Protein photodegradation in the fluorescence unfolding kinetics study of bromelain
Volume: 7 Issue: 2
Author(s): Alfonso Arroyo-Reyna*Salvador R. Tello-Solis
Affiliation:
- Area de Biofisicoquimica, Departamento de Quimica, Universidad Aut6noma Metropolitana-Iztapalapa, Apartado Postal 55-534, Iztapalapa 09340, D.F., Mexico
Abstract: We have detected protein photodegradation in the fluorescence unfolding kinetics experiment of stem bromelain, a cysteine proteinase from the papain family. Thermally induced unfolding has been followed by near and far circular dichroism and tryptophan fluorescence emission. It was found that the fluorescence kinetics involves two phases. This biphasic nature results from ultraviolet induced photolysis oftryptophan.
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Cite this article as:
Arroyo-Reyna Alfonso*, Tello-Solis R. Salvador, Protein photodegradation in the fluorescence unfolding kinetics study of bromelain, Protein & Peptide Letters 2000; 7 (2) . https://dx.doi.org/10.2174/092986650702221206114551
DOI https://dx.doi.org/10.2174/092986650702221206114551 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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