Interprotein metal ion exchange between cadmium-carbonic anhydrase and apo- or zinc-metallothionein |
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Authors: | John Ejnik Amalia Muñoz Tong Gan C. Frank Shaw III D. H. Petering |
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Affiliation: | (1) Department of Chemistry, University of Wisconsin-Milwaukee P.O. Box 413, Milwaukee, WI 53201, USA e-mail: petering@uwm.edu Tel.: +1-414-229853 Fax: +1-414-2295530, US |
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Abstract: | − 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. Received: 25 February 1999 / Accepted: 17 September 1999 |
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Keywords: | Cadmium-carbonic anhydrase Apometallothionein Zinc-metallothionein Metal ion exchange |
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