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A micro-scale method for determining relative metal-binding affinities of proteins

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Abstract

This article describes a quick and easy method for determining relative binding affinities between proteins and metal ions. The method is based on separating unbound metal ions from metal ions bound to protein by ultrafiltration using microcentrifuge ultrafiltration units. Bovine serum albumin (BSA) was used as the test protein and the relative affinity towards divalent metal ions was found to be Cu2+>Zn2+>Cd2+>Pb2+>Ni2+>Co2+, which corresponds to the relative orders reported in the literature.

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Authors and Affiliations

  1. Jens Sommer-Knudsen, Plant Cell Biology Research Centre, School of Botany, University of Melbourne, 3052, Parkville, Victoria, Australia

    Jens Sommer-Knudsen & Antony Bacic

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  1. Jens Sommer-Knudsen
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  2. Antony Bacic
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Correspondence to Jens Sommer-Knudsen.

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Sommer-Knudsen, J., Bacic, A. A micro-scale method for determining relative metal-binding affinities of proteins. Mol Biotechnol 8, 215–218 (1997). https://doi.org/10.1007/BF02760774

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