Abstract
Green fluorescent protein (GFP) is widely used as an excellent reporter molecule in biochemistry and cell biology. Some biochemical and immunological assays require high-purity GFP. However, the majority of current procedures for GFP purification include multiple time-consuming chromatography steps with a low yield of the desired product or require tag-containing proteins. An alternative method is described for the GFP purification without affinity extensions using organic extraction yielding a highly homogeneous protein indistinguishable in spectroscopic properties from that purified by previous methods.
Copyright 1998 Academic Press.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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1-Butanol
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Ammonium Sulfate
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Chemical Fractionation
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Chemical Precipitation
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Chloroform
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Chromatography, Liquid
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Circular Dichroism
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Escherichia coli / genetics
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Ethanol
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Green Fluorescent Proteins
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Luminescent Proteins / genetics
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Luminescent Proteins / isolation & purification*
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / isolation & purification*
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Sepharose / analogs & derivatives
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Solvents
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Spectrometry, Fluorescence
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Water
Substances
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Luminescent Proteins
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Recombinant Fusion Proteins
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Solvents
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Water
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Green Fluorescent Proteins
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Ethanol
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phenyl-sepharose
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Chloroform
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1-Butanol
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Sepharose
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Ammonium Sulfate