ESR determination of the thermal stability of Mn2+ ion binding sites in different legume lectins

2009 ◽  
Vol 35 (4) ◽  
pp. 593-599 ◽  
Author(s):  
Mustafa Coşkun ◽  
M. Korkmaz
Keyword(s):  
Thermal Stability ◽  
Binding Sites ◽  
Ion Binding ◽  
Ion Binding Sites ◽  
Legume Lectins ◽  
Thermal Stability Of

Determination of Metal Ion Binding Sites within the Hairpin Ribozyme Domains by NMR†

Biochemistry ◽  
2000 ◽  
Vol 39 (9) ◽  
pp. 2174-2182 ◽  
Author(s):  
Samuel E. Butcher ◽  
Frédéric H.-T. Allain ◽  
Juli Feigon
Keyword(s):  
Binding Sites ◽  
Metal Ion ◽  
Ion Binding ◽  
Hairpin Ribozyme ◽  
Metal Ion Binding ◽  
Ion Binding Sites ◽  
Metal Ion Binding Sites

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.

Determination of the Thermal Stability of Explosives

2021 ◽  
Vol 15 (2) ◽  
pp. 271-277
Author(s):  
G. M. Nazin ◽  
B. L. Korsunskiy
Keyword(s):  
Thermal Stability ◽  
Thermal Stability Of

scholarly journals Synthesis and Photoregulated Metal Coordination of Azobenzene Polymer Having Ion Binding Sites

1991 ◽  
Vol 23 (2) ◽  
pp. 127-134 ◽  
Author(s):  
Masato Nanasawa ◽  
Takahiro Nishiyama ◽  
Hiroyoshi Kamogawa
Keyword(s):  
Binding Sites ◽  
Metal Coordination ◽  
Ion Binding ◽  
Azobenzene Polymer ◽  
Ion Binding Sites
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