Abstract
Due to asymmetrical charge distribution of the mammalian high mobility group protein A2 (HMGA2), which makes HMGA2 bind to both cation- and anion-exchange columns, we developed a rapid procedure for purifying HMGA2 in the milligram range. This purification procedure greatly facilitated biophysical studies, which require large amounts of the protein.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Chromatography, Ion Exchange
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Gene Expression
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HMGA2 Protein / biosynthesis
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HMGA2 Protein / chemistry*
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HMGA2 Protein / genetics
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HMGA2 Protein / isolation & purification*
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Molecular Sequence Data
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry*
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification*
Substances
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HMGA2 Protein
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Recombinant Proteins