Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/195763
Type: Artigo de periódico
Title: Effect Of Chaotropic Agents On Reversible Unfolding Of A Soybean (glycine Max) Seed Acid Phosphatase.
Author: Cavagis, Alexandre Donizeti Martins
Granjeiro, Paulo Afonso
Ferreira, Carmen Veríssima
Aoyama, Hiroshi
Abstract: In this work we examined the effect of urea and guanidinium chloride on the structural stability of a single isoform of soybean seed acid phosphatase, based on the intensity of tryptophan fluorescence as a function of denaturant concentration. The free energy of unfolding, DeltaGu, was calculated at 25 degrees C as a function of the concentrations of both chaotropic agents; the conformational stability, DeltaG (H2O), was determined to be 2.48 kcal mol(-1). Center of mass, determined from analysis of fluorescence data, was used as a parameter to assess conformational changes. Our results indicate that complete enzyme inactivation occurred before full enzyme unfolding in both cases, and suggest that there are differences between the conformational flexibility of the active-site and that of the macromolecule as a whole.
Subject: Acid Phosphatase
Guanidine
Protein Denaturation
Protein Folding
Seeds
Soybeans
Spectrometry, Fluorescence
Thermodynamics
Urea
Rights: fechado
Identifier DOI: 10.1016/j.phytochem.2004.02.004
Address: http://www.ncbi.nlm.nih.gov/pubmed/15081282
Date Issue: 2004
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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