Abstract
We report a straightforward methodology for purification of recombinant proteins by incorporating a short hydrophilic peptide marker segment at their N-termini. A calcium-dependent antibody that reacts primarily with the first three amino acids of this peptide segment was used to affinity purify the fusion proteins in a single chromatographic step. The marker peptide could subsequently be removed by proteolysis with the enzyme enterokinase.
MeSH terms
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Antibodies, Monoclonal*
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Calcium*
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Chromatography, Affinity / methods*
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Enteropeptidase
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Genetic Vectors
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Interleukin-3 / genetics
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Interleukin-3 / isolation & purification*
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Interleukin-4 / genetics
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Interleukin-4 / isolation & purification*
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Plasmids
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Recombinant Proteins / isolation & purification*
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Saccharomyces cerevisiae
Substances
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Antibodies, Monoclonal
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Interleukin-3
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Recombinant Proteins
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Interleukin-4
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Enteropeptidase
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Calcium