Premium
Calcyclin is a calcium and zinc binding protein
Author(s) -
Filipek Anna,
Heizmann Claus W.,
Kúznicki Jacek
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80263-i
Subject(s) - calcium , zinc , chemistry , binding site , calcium binding protein , dimer , biophysics , tyrosine , binding protein , plasma protein binding , biochemistry , monomer , biology , organic chemistry , gene , polymer
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.