Table 3.

Dissociation constants of I-domains for protein ligands



Kd, μM
Ligand
αD active
αD nonactive
αLD) chimera
αL active
Fibrinogen   0.76 ± 0.63   ND   1.45 ± 0.57   ND  
Vitronectin   1.03 ± 0.41   ND   2.32 ± 0.71   ND  
Fibronectin   0.38 ± 0.14   ND   1.99 ± 0.54   ND  
Cyr61   0.29 ± 0.07   ND   0.96 ± 0.27   ND  
Plasminogen   0.96 ± 0.34   ND   2.0 ± 0.41   ND  
VCAM-1   8.13 ± 0.91   ND   8.58 ± 0.56   ND  
ICAM-3
 
1.89 ± 1.3
 
ND
 
6.83 ± 0.72
 
1.01 ± 0.24
 


Kd, μM
Ligand
αD active
αD nonactive
αLD) chimera
αL active
Fibrinogen   0.76 ± 0.63   ND   1.45 ± 0.57   ND  
Vitronectin   1.03 ± 0.41   ND   2.32 ± 0.71   ND  
Fibronectin   0.38 ± 0.14   ND   1.99 ± 0.54   ND  
Cyr61   0.29 ± 0.07   ND   0.96 ± 0.27   ND  
Plasminogen   0.96 ± 0.34   ND   2.0 ± 0.41   ND  
VCAM-1   8.13 ± 0.91   ND   8.58 ± 0.56   ND  
ICAM-3
 
1.89 ± 1.3
 
ND
 
6.83 ± 0.72
 
1.01 ± 0.24
 

Different concentrations of I-domains ranging from 0.05 to 16 μM in HBS-P buffer supplemented with 1 mM MgCl2 were flowed over the flow cells with immobilized protein ligands. The Kd values were estimated from the equilibrium portions of sensograms using the BIA evaluation 3.1 program. Results are mean ± SE of 3 to 5 individual determinations. ND indicates no significant binding was detected.

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