Zinc forms complexes with higher kinetical stability than calcium, 5-F-BAPTA as a good example
- 1 December 1989
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 165 (2) , 838-844
- https://doi.org/10.1016/s0006-291x(89)80042-7
Abstract
No abstract availableThis publication has 51 references indexed in Scilit:
- Carboxylate-histidine-zinc interactions in protein structure and functionJournal of the American Chemical Society, 1989
- Zinc increases the affinity of phorbol ester receptor in T lymphocytesBiochemical and Biophysical Research Communications, 1988
- Calcium complexation with a highly calcium selective chelator: crystal structure of ca(CaFBAPTA) ·5H2OJournal of Inorganic Biochemistry, 1987
- The Complete Primary Structure of Protein Kinase C—the Major Phorbol Ester ReceptorScience, 1986
- Potential Metal-Binding Domains in Nucleic Acid Binding ProteinsScience, 1986
- Free cytosolic Ca2+ measurements with fluorine labelled indicators using 19FNMRCell Calcium, 1985
- Calcium ChannelAnnual Review of Neuroscience, 1981
- Zinc-dependent action potentials in giant neurons of the snail,Euhadra quaestiaThe Journal of Membrane Biology, 1979
- Calcium-Binding ProteinsAnnual Review of Biochemistry, 1976
- Ion Transport by Heart MitochondriaJournal of Biological Chemistry, 1967