ISSN:
1432-1327
Keywords:
Cadmium-carbonic anhydrase
;
Apometallothionein
;
Zinc-metallothionein
;
Metal ion exchange
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
− 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s007750050351
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