Use este identificador para citar ou linkar para este item: https://repositorio.inpa.gov.br/handle/1/18836
Título: One-step purification of metallothionein extracted from two different sources
Autor: Honda, Rubens Tomio
Araújo, Roziete Mendes
Horta, Bruno Brasil
Val, Adalberto Luis
Demasi, Marilene
Palavras-chave: Chelation
Chromatographic Analysis
Extraction
Proteins
Purification
Ultraviolet Spectroscopy
Yeast
Apoproteins
Metal-chelating Columns
Metallothionein
Saccharomyces Cerevisiae
Organometallics
Apoprotein
Cadmium
Copper
Edetic Acid
Imidazole
Metallothionein
Resin
Chromatography, Affinity
Animals Experiment
Animals Tissue
Chemical Procedures
Colossoma Macroponum
Controlled Study
Elution
Extraction
Fish
Nonhuman
Electrophoresis, Polyacrylamide Gel
Priority Journal
Protein Purification
Saccharomyces Cerevisiae
Ultraviolet Spectroscopy
Yeast
Animal
Electrophoresis, Polyacrylamide Gel
Fishes
Metallothionein
Spectrophotometry, Ultraviolet
Colossoma Macropomum
Pisces
Saccharomyces Cerevisiae
Data do documento: 2005
Revista: Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
É parte de: Volume 820, Número 2, Pags. 205-210
Abstract: We describe a one-step purification of hepatic metallothionein from the Amazon fish Colossoma macropomum injected with cadmium and from the copper-loaded metallothionein from the yeast Saccharomyces cerevisiae, performed by affinity chromatography through metal-chelating columns. Yeast metallothionein was purified from Cu2+-loaded resin and eluted by a continuous EDTA gradient whereas hepatic metallothionein extracted from fishes was purified by Ni2+-loaded resin and eluted by a continuous imidazol gradient. Purified metallothioneins were evaluated by SDS-PAGE and characterized by UV spectra of the apo- and Cd2+-loaded protein. This method allowed high purity and yield as well as rapid one-step extraction of both metal-loaded and apoprotein. © 2005 Elsevier B.V. All rights reserved.
DOI: 10.1016/j.jchromb.2005.03.017
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