Terbium ion binding to a synthetic .gamma.-carboxyglutamic acid containing heptapeptide corresponding to bovine prothrombin residues 17-23

1986 ◽  
Vol 25 (25) ◽  
pp. 4503-4506 ◽  
Author(s):  
Henry C. Marsh ◽  
Randal A. Hoke ◽  
David W. Deerfield ◽  
Lee G. Pedersen ◽  
Richard G. Hiskey ◽  
...  
Keyword(s):  
Ion Binding ◽  
Carboxyglutamic Acid ◽  
Terbium Ion

ChemInform Abstract: Terbium Ion Binding to a Synthetic γ-Carboxyglutamic Acid Containing Heptapeptide Corresponding to Bovine Prothrombin Residues 17-23.

ChemInform ◽  
1987 ◽  
Vol 18 (16) ◽  
Author(s):  
H. C. JUN. MARSH ◽  
R. A. HOKE ◽  
D. W. II DEERFIELD ◽  
L. G. PEDERSEN ◽  
R. G. HISKEY ◽  
...  
Keyword(s):  
Ion Binding ◽  
Carboxyglutamic Acid ◽  
Terbium Ion

Terbium ion binding to Limuluspolyphemus hemocyanin

1981 ◽  
Vol 100 (3) ◽  
pp. 1305-1313 ◽  
Author(s):  
Beth E. Nelson ◽  
Susan J. Gan ◽  
Kenneth G. Strothkamp
Keyword(s):  
Ion Binding ◽  
Terbium Ion

DETERMINATION OF NUMBER OF γ-CARBOXYGLUTAMIC ACID (GLA) RESIDUES INVOLVED IN FORMING THE TWO HIGH AFFINITY METAL BINDING SITES IN PROTHROMBIN AND FACTOR X

1987 ◽  
Author(s):  
G L Brodsky ◽  
S P Bajaj
Keyword(s):  
Metal Binding ◽  
Binding Sites ◽  
Ion Binding ◽  
Factor X ◽  
Metal Binding Sites ◽  
High Affinity ◽  
Carboxyglutamic Acid ◽  
High Affinity Site ◽  
Ion Binding Sites

Prothrombin and factor X possess two high affinity and several low affinity lanthanide ion binding sites. In both proteins, the association constant of the high affinity sites is at least 50-fold greater than that of the low affinity sites. Moreover, metal bound to these high affinity sites is extremely difficult to displace. It has been proposed that one of the two high affinity sites in factor X involves Gla residues while the other involves β-hydroxyaspartic acid and no Gla residues. It is also known that ^H can be specifically incorporated into Gla residues at an acidic pH. We have determined that under nondenaturing conditions when Gla (synthetic or in proteins) is complexed to metal at pH 5.5, this specific 3H incorporation is blocked. Furthermore, we have found that β-hydroxyaspartic acid does not incorporate in the presence or absence of metal. When we incubated prothrombin or factor X (41 μM) with 3H2O in the presence of Tb3+ or Gd3+ (82 μM), we blocked 5.6 Gla residues per prothrombin and 5.5 Gla residues per factor X from 3H incorporation. Under these conditions, we calculated that >95% of the high affinity sites are occupied by metal. Thus, in prothrombin, an average of 2.8 Gla residues are involved in forming each high affinity site. If the Gla residues in factor X participate in forming only one of the two high affinity sites, then all 5.5 Gla residues blocked from incorporation must be involved in forming that site. However, this seems highly unlikely. We conclude that, as in prothrombin, both high affinity sites in factor X involve Gla residues (average 2.75/site). However, our data does not exclude the possibility of existence of a heterologous site containing both β-hydroxyaspartic acid and Gla residues.

Photophysical Characterisation, Metal Ion Binding and Enantiomeric Recognition of Chiral Ligands Containing Phenazine Fluorophore

2004 ◽  
Vol 69 (4) ◽  
pp. 885-896 ◽  
Author(s):  
Luisa Stella Dolci ◽  
Péter Huszthy ◽  
Erika Samu ◽  
Marco Montalti ◽  
Luca Prodi ◽  
...  
Keyword(s):  
Metal Ion ◽  
Photophysical Properties ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Ammonium Ions ◽  
Enantiomerically Pure ◽  
Binding Process ◽  
High Affinity ◽  
Enantiomeric Recognition ◽  
Chiral Species

Enantiomerically pure dimethyl- and diisobutyl-substituted phenazino-18-crown-6 ligands bind metal and ammonium ions and also primary aralkylammonium perchlorates in acetonitrile with high affinity, causing pronounced changes in their luminescence properties. In addition, they show enantioselectivity towards chiral primary aralkylammonium perchlorates. The possibility to monitor the binding process by photoluminescence spectroscopy can gain ground for the design of very efficient enantioselective chemosensors for chiral species. The observed changes in the photophysical properties are also an important tool for understanding the interactions present in the adduct.

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