| First Author | Filipek A | Year | 1990 |
| Journal | FEBS Lett | Volume | 264 |
| Issue | 2 | Pages | 263-6 |
| PubMed ID | 2358072 | Mgi Jnum | J:113706 |
| Mgi Id | MGI:3687445 | Doi | 10.1016/0014-5793(90)80263-i |
| Citation | Filipek A, et al. (1990) Calcyclin is a calcium and zinc binding protein. FEBS Lett 264(2):263-6 |
| abstractText | 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 Ca2+ lacks effect on the binding of Zn2+, and Ca2+ (but not Zn2+) increases tyrosine fluorescence intensity. Binding of Zn2+ reduces the extent of the conformational changes induced by Ca2+, and seems to affect Ca2(+)-binding. The data suggest that Ca2+ and Zn2+ might trigger the biological activity of calcyclin. |
