− 1
s − 1 at 25 °C and pH 7.4 in Tris.HCl buffer and 0.1 M KCl. At 25 °C, Zn7-metallothionein also exchanged metal ions with Cd-carbonic anhydrase with a rate constant of 0.33 ± 0.02 M − 1 s − 1 to reconstitute enzymatically active protein. Cd-carbonic anhydrase reacted within the time of mixing with the peptide sequence 49–61 of rabbit metallothionein 2 which contains four cysteinyl residues, leading to the exchange of most of the Cd2+ into the peptide. At pH 7.4 and 25 °C, Cd2+ has higher affinity for apometallothionein than for the apo-peptide.
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Received: 25 February 1999 / Accepted: 17 September 1999
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Ejnik, J., Muñoz, A., Gan, T. et al. Interprotein metal ion exchange between cadmium-carbonic anhydrase and apo- or zinc-metallothionein. JBIC 4, 784–790 (1999). https://doi.org/10.1007/s007750050351
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DOI: https://doi.org/10.1007/s007750050351