PMID: 2510714Aug 15, 1989Paper

Domain-specificity of Cd2+ and Zn2+ binding to rabbit liver metallothionein 2. Metal ion mobility in the formation of Cd4-metallothionein alpha-fragment

The Biochemical Journal
M J Stillman, A J Zelazowski

Abstract

The yield of the alpha-fragment of rabbit liver metallothionein 2 was used to test the domain-specificity and mobility of Cd2+ and Zn2+ when bound to metallothionein. Increasing molar ratios of Cd2+ were added to either Zn7-metallothionein or the metal-ion-free apo-metallothionein. The enzyme subtilisin was used to digest those parts of the peptide chain that were not bound to Cd2+. Analysis of the digestion products was carried out by separation by polyacrylamide-gel electrophoresis. The chelation agent EDTA was used as a competitive chelator. It was found that the presence of excess EDTA greatly enhances the formation of the Cd4-metallothionein alpha-fragment, and catalyses the complete digestion of all other the metal-ion-containing peptides, so that even Cd7-metallothionein, formed when 7 molar equivalents of Cd2+ are added to Zn7-metallothionein, is digested to the alpha-fragment. These results suggest that the Cd2+ bound in the beta-sites is very labile, much more labile than the kinetics of the off-reaction would suggest. The observation of significant amounts of alpha-fragment on the gels, even when the stoichiometry of the metal ions initially present in the protein should not have resulted in much concentration of Cd4...Continue Reading

Citations

May 4, 2017·Metallomics : Integrated Biometal Science·Judith S SchellerMartin J Stillman
Mar 29, 2007·The FEBS Journal·Kelly E Rigby Duncan, Martin J Stillman
Jan 23, 2002·Journal of Inorganic Biochemistry·John EjnikDavid H Petering
Nov 16, 2002·Journal of Inorganic Biochemistry·Zhong Xian HuangPeng Yuan Yang
Sep 11, 1992·Toxicology and Applied Pharmacology·J M McKimC D Klaassen

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