Function of N-[(9-.beta.-D-ribofuranosyl)purin-6-yl)carbamoyl]threonine in transfer ribonucleic acid. Metal ion binding studies

Biochemistry ◽  
1981 ◽  
Vol 20 (17) ◽  
pp. 4979-4986 ◽  
Author(s):  
P. Rabindra Reddy ◽  
W. David Hamill ◽  
Girish B. Chheda ◽  
Martin P. Schweizer
Keyword(s):  
Ribonucleic Acid ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Studies

Bromine substituted aminonaphthoquinones: synthesis, characterization, DFT and metal ion binding studies

RSC Advances ◽  
2016 ◽  
Vol 6 (91) ◽  
pp. 88010-88029 ◽  
Author(s):  
Gunjan Agarwal ◽  
Dipali N. Lande ◽  
Debamitra Chakrovarty ◽  
Shridhar P. Gejji ◽  
Prajakta Gosavi-Mirkute ◽  
...  
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Studies

Bromine substituted aminonaphthoquinones – chemosensors for metal ions.

New Fluorescence PET Systems Based on N2S2Pyridine-Anthracene-Containing Macrocyclic Ligands. Spectrophotometric, Spectrofluorimetric, and Metal Ion Binding Studies

2005 ◽  
Vol 44 (22) ◽  
pp. 8105-8115 ◽  
Author(s):  
Abel Tamayo ◽  
Carlos Lodeiro ◽  
Lluis Escriche ◽  
Jaume Casabó ◽  
Berta Covelo ◽  
...  
Keyword(s):  
Metal Ion ◽  
Macrocyclic Ligands ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Studies

Bis-amino Acid Derivatives of 1,1′-Ferrocenedicarboxylic Acid: Structural, Electrochemical, and Metal Ion Binding Studies

2014 ◽  
Vol 33 (18) ◽  
pp. 4873-4887 ◽  
Author(s):  
Bimalendu Adhikari ◽  
Alan J. Lough ◽  
Bryan Barker ◽  
Afzal Shah ◽  
Cuili Xiang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Metal Ion ◽  
Amino Acid Derivatives ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Studies ◽  
Derivatives Of

scholarly journals The formation of ferritin from apoferritin. Inhibition and metal ion-binding studies

1973 ◽  
Vol 135 (4) ◽  
pp. 785-789 ◽  
Author(s):  
Ian G. Macara ◽  
Terence G. Hoy ◽  
Pauline M. Harrison
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Iron Uptake ◽  
Metal Ion ◽  
External Surface ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Studies ◽  
Titration Data ◽  
Substrate Concentrations

Inhibition by Zn2+of iron uptake by apoferritin at very low substrate concentrations is shown to be competitive. It is proposed that Zn2+competes with Fe2+for sites on the protein at which the oxidation of Fe2+is catalysed. Interpretation of titration data suggests there are two independent classes of binding site for Zn2+and several other cations. Sites in one such class are probably on the external surface of the apoferritin molecule. The catalytic binding sites are presumed to be internal and may involve histidine or possibly cysteine as ligands.

scholarly journals Kinetic and equilibrium metal-ion-binding behaviour reflected in a metal-ion-dependent antigenic determinant in bovine prothrombin. Comparison with bovine prothrombin fragment 1

1981 ◽  
Vol 193 (2) ◽  
pp. 411-418 ◽  
Author(s):  
D A Madar ◽  
T J Hall ◽  
R G Hiskey ◽  
K A Koehler
Keyword(s):  
Metal Ions ◽  
Protein Conformation ◽  
Metal Ion ◽  
Ion Binding ◽  
Conformation Change ◽  
Metal Ion Binding ◽  
Binding Studies ◽  
Prothrombin Fragment ◽  
Absolute Requirement ◽  
Binding Behaviour

Rabbit anti-(bovine prothrombin fragment 1) antibodies were fractionated by using fragment-1 affinity chromatography in the absence of metal ions, and showed an absolute requirement for the presence of metal ions in their interactions with bovine fragment 1 or prothrombin. These antibodies were employed to evaluate both the rate constants for a protein conformation change and the equilibrium metal-ion binding to isolated bovine fragment 1 and intact prothrombin. The close similarity of the rates obtained for the conformation change in fragment 1 and those observed in prothrombin indicated that the same process is involved in both proteins and that the non-fragment-1 region of the prothrombin has essentially no effect on this process in the fragment-1 region. Equilibrium metal-ion-binding studies indicate that the details of the metal-ion-binding process in fragment 1 and prothrombin are essentially the same. We conclude that the metal-ion-binding behaviour of the fragment-1 domain of intact prothrombin is identical with that of isolated fragment 1.

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