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Metal-affinity partitioning of phosphoproteins in PEG/dextran two-phase systems

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Summary

Ferric ion (Fe3+) complexed to iminodiacetic acid (IDA)-polyethylene glycol enhances the partitioning of phosphoproteins in PEG/dextran aqueous two-phase systems. The ratio of partition coefficients in the presence and absence of Fe(III)IDA-PEG, K/K0, is highly sensitive to pH, increasing in the pH range of 3.0 to 5.0 and decreasing rapidly with a further increase in pH. The steep decline in partition coefficients above pH 5 can be explained by inhibitory binding of hydroxyl ions to ferric ion. In metal-affinity partitioning of phosvitin, the most highly phosphorylated protein known, K/K0≫1,000 was obtained. This is one of the highest values reported for affinity partitioning.

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Authors and Affiliations

  1. Division of Chemistry and Chemical Engineering 210-41, California Institute of Technology, 91125, Pasadena, CA

    Bong Hyun Chung & Frances H. Arnold

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  1. Bong Hyun Chung
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  2. Frances H. Arnold
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Chung, B.H., Arnold, F.H. Metal-affinity partitioning of phosphoproteins in PEG/dextran two-phase systems. Biotechnol Lett 13, 615–620 (1991). https://doi.org/10.1007/BF01033420

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  • DOI: https://doi.org/10.1007/BF01033420

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