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Last Updated: 3 years ago

Possible Interaction: Cupric Cation and Zinc Cation

supplement:

Cupric Cation

supplement:

Zinc Cation

Research Papers that Mention the Interaction

Common multivalent cations present in biological systems like Al3+, Cu2+ , Fe3+, Ca2+, and Mg2+, interfered with the measurement of Zn(II ) only when present in excess of 20, 33, 60, 500 and 30,000 times the Zn (II) concentration, respectively.
Biological research  •  1994  |  View Paper
When aggregates are prepared in the copresence of Cu(II) and Zn(II) ions , the ratio of Cu(II):Zn(II) becomes an important factor in the degeneration of H2O2, the formation of carbonyl groups in the peptide, and in aggregate morphology.
The Journal of Biological Chemistry  •  2014  |  View Paper
20 times enhancement in fluorescence intensity on interaction with Zn2+ , due to snapping of photoinduced electron transfer (PET) process, which is selective over metal ions - Na+, K+, Ca2+, Ni2+, Cu2+ , Cd2+, Hg2+ and Pb2+.
Journal of Fluorescence  •  2013  |  View Paper
From these studies, we suggest that Abeta-chelated Zn(II) is readily displaced by Cu(II) and Fe(III) ions and leads to a propagation of oxidative stress.
Journal of Alzheimer's disease : JAD  •  2010  |  View Paper
Zn(II ) promoted L55P amyloid formation at pH 7.4 but Cu(II) inhibited it.
Biochemistry  •  2007  |  View Paper
Zn(II ) inhibited whilst Cu(II) prevented the formation of beta-pleated sheets of Abeta42and neither of these influences were affected by incubation of the aged peptide aggregates with either DFO or EDTA.
Journal of Alzheimer's disease : JAD  •  2004  |  View Paper
Plasma ceruloplasmin (added to the basal chamber) failed to enhance basolateral iron release, and Zn(II ) failed to compete with Cu(II ) for uptake.
Biometals  •  2004  |  View Paper
Conclusion: Our results suggest that the Zn(II) and Cu(II) complexes display significant MDR-reversing activity in a dose-dependent manner and possess strong cytotoxic activity and a remarkable potential to induce apoptosis in MDR L5178Y mouse T-lymphoma cells.
AntiCancer Research  •  2018  |  View Paper
Here we show that Zn(II) and Cu(II) inhibit Aβ42 fibrillization and initiate formation of non‐fibrillar Aβ42 aggregates, and that the inhibitory effect of Zn(II) (IC50 = 1.8 μmol/L) is three times stronger than that of Cu(II).
Journal of neurochemistry  •  2009  |  View Paper
Transmural S to M transport of 65Zn2+ was markedly reduced with the addition of the serosal inhibitors ouabain (32%), excess K+ (25%), excess Ca2+ (30%), Cu2+ (38%), nifedipine (21%), and vanadate (53%).
Journal of Comparative Physiology B  •  2006  |  View Paper
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