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Calcyclin is a calcium and zinc binding protein

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
264
Issue
2
Identifiers
DOI: 10.1016/0014-5793(90)80263-i
Keywords
  • Calcyclin
  • Calcium-Binding Protein
  • Zinc-Binding Protein
Disciplines
  • Biology

Abstract

Abstract Calcyclin, a cell cycle regulated protein, was recently purified from Ehrlich ascites tumour (EAT) cells and shown to be a calcium binding protein. Here we show that calcyclin monomer and dimer also bind zinc ions. Zinc binding sites seem to be different from calcium binding sites since: preincubation with Ca 2+ lacks effect on the binding of Zn 2+, and Ca 2+ (but not Zn 2+) increases tyrosine fluorescence intensity. Binding of Zn 2+ reduces the extent of the conformational changes induced by Ca 2+, and seems to affect Ca 2+-binding. The data suggest that Ca 2+- and Zn 2+- might trigger the biological activity of calcyclin.

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