Interactions of DNA with divalent metal ions. III. Extent of metal binding: Experiment and theory

Biopolymers ◽  
1982 ◽  
Vol 21 (1) ◽  
pp. 219-232 ◽  
Author(s):  
Joseph Granot ◽  
David R. Kearns
Keyword(s):  
Metal Ions ◽  
Metal Binding ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Binding Experiment

scholarly journals Regulation of divalent metal ions to the aggregation and membrane damage of human islet amyloid polypeptide oligomers

RSC Advances ◽  
2021 ◽  
Vol 11 (21) ◽  
pp. 12815-12825
Author(s):  
Yajie Wang ◽  
Feihong Meng ◽  
Tong Lu ◽  
Chunyun Wang ◽  
Fei Li
Keyword(s):  
Metal Ions ◽  
Metal Binding ◽  
Membrane Damage ◽  
Islet Amyloid Polypeptide ◽  
Divalent Metal ◽  
Human Islet ◽  
Divalent Metal Ions ◽  
Islet Amyloid ◽  
Induced Membrane ◽  
Human Islet Amyloid Polypeptide

Their is a counteraction between a decrease in the disruptive ability of metal-associated oligomer species and an increase in the quantity of oligomers promoted by the metal binding in the activity of hIAPP induced membrane damage.

scholarly journals MOTOR END PLATE REACTIVITY TO DIVALENT METAL IONS HISTOCHEMICAL STUDIES

1967 ◽  
Vol 15 (5) ◽  
pp. 276-284 ◽  
Author(s):  
TOSHIO NAKAMURA ◽  
TATSUJI NAMBA ◽  
DAVID GROB
Keyword(s):  
Metal Ions ◽  
Metal Binding ◽  
Calcium Release ◽  
Cholinesterase Activity ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Alizarin Red ◽  
End Plate ◽  
Motor End Plate

Motor end plates in the tibialis anterior muscle of the rat were demonstrated by metal sulfide deposits following injection of aqueous solutions of lead, stannous, cadmium, zinc or cupric ions into the muscle in vivo or in vitro. The appearance of the end plates was similar to the structure demonstrated by cholinesterase staining, with visualization of the subneural apparatus. Neither metal binding nor cholinesterase activity was affected 4 weeks after dissection of the sciatic nerve, indicating that the metal binding site is postsynaptic. Freezing or formalin fixation of muscle prevented binding of all metal ions to the end plate without greatly affecting cholinesterase activity, indicating that these two activities of the end plate are distinct. Prior administration of acetylcholine, d-tubocurarine, neostigmine or diisopropyl fluorophosphate inhibited binding to the end plate of cadmium and zinc ions but did not alter binding of lead and stannous ions. By formation of a lake with alizarin red S previously injected in vivo intramuscularly, the release of calcium ions at the motor end plate following stimulation of the muscle through the nerve or administration of neostigmine was demonstrated. These results suggest a close relationship of the site of binding of divalent metal ions in the motor end plate to the site of calcium release, and a close but not identical relationship to the site of cholinesterase activity and the acetylcholine receptor.

Influence of monovalent metal ions on metal binding and catalytic activity of the 10–23 DNAzyme

2020 ◽  
Vol 402 (1) ◽  
pp. 99-111
Author(s):  
Hannah Rosenbach ◽  
Jan Borggräfe ◽  
Julian Victor ◽  
Christine Wuebben ◽  
Olav Schiemann ◽  
...  
Keyword(s):  
Metal Ions ◽  
Metal Binding ◽  
Divalent Cations ◽  
Reaction Rates ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Monovalent Metal ◽  
Biophysical Techniques ◽  
Target Rna

AbstractDeoxyribozymes (DNAzymes) are single-stranded DNA molecules that catalyze a broad range of chemical reactions. The 10–23 DNAzyme catalyzes the cleavage of RNA strands and can be designed to cleave essentially any target RNA, which makes it particularly interesting for therapeutic and biosensing applications. The activity of this DNAzyme in vitro is considerably higher than in cells, which was suggested to be a result of the low intracellular concentration of bioavailable divalent cations. While the interaction of the 10–23 DNAzyme with divalent metal ions was studied extensively, the influence of monovalent metal ions on its activity remains poorly understood. Here, we characterize the influence of monovalent and divalent cations on the 10–23 DNAzyme utilizing functional and biophysical techniques. Our results show that Na+ and K+ affect the binding of divalent metal ions to the DNAzyme:RNA complex and considerably modulate the reaction rates of RNA cleavage. We observe an opposite effect of high levels of Na+ and K+ concentrations on Mg2+- and Mn2+-induced reactions, revealing a different interplay of these metals in catalysis. Based on these findings, we propose a model for the interaction of metal ions with the DNAzyme:RNA complex.

Interaction of divalent metal ions with the NADP+-malic enzyme from maize leaves

1991 ◽  
Vol 81 (4) ◽  
pp. 462-466 ◽  
Author(s):  
Maria Fabiana Drincovich ◽  
Alberto A. Iglesias ◽  
Carlos S. Andreo
Keyword(s):  
Metal Ions ◽  
Malic Enzyme ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Maize Leaves
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