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

Molecular Biotechnology
J Sommer-Knudsen, A Bacic

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.

References

Jan 1, 1988·Methods in Enzymology·B Holmquist
Jan 1, 1974·Journal of Clinical Pathology·D J GoldieG K McGowan
Jul 1, 1981·Journal of Inorganic Biochemistry·E Giroux, J Schoun

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Citations

Feb 20, 2013·The Journal of Physiology·Alina MarandykinaFeliksas F Bukauskas
Jul 22, 2008·Acta Biologica Hungarica·Houda BouaziziE El Ferjani
Mar 8, 2011·Journal of Colloid and Interface Science·Alla N GeneralovaVitali P Zubov
Mar 10, 2017·Nanoscale·Pasquale BoveStefania Sabella

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