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Table 1 Kinetic parameters of the interaction between human CXCL10 proteoforms and GAGs

From: Natural carboxyterminal truncation of human CXCL10 attenuates glycosaminoglycan binding, CXCR3A signaling and lymphocyte chemotaxis, while retaining angiostatic activity

 

Heparan sulfate

Heparin

Chondroitin sulfate A

Chemokine

kon (1/M.s)

koff (1/s)

Apparent KD (nM)

kon (1/M.s)

koff (1/s)

Apparent KD (nM)

kon (1/M.s)

koff (1/s)

Apparent KD (nM)

CXCL4

(8.58 ± 0.54) E+ 05

(3.21 ± 0.14)

E-03

3.75 ± 0.10

N.D.

N.D.

N.D.

(4.36 ± 0.60) E+ 05

(6.71 ± 0.77)

E-03

15.91 ± 2.61

CXCL10(1–77)

(5.28 ± 0.84) E+ 05

(3.41 ± 0.43)

E-03

6.73 ± 0.65

(9.76 ± 0.41) E+ 05

(1.00 ± 0.04)

E-03

1.03 ± 0.01

(1.69 ± 0.09) E+ 05

(5.57 ± 0.34)

E-03

33.40 ± 2.86

CXCL10(1–73)

(4.86 ± 0.96) E+ 04

(1.26 ± 0.27)

E-03

25.23 ± 1.16

(4.26 ± 0.32) E+ 04

(1.39 ± 0.04)

E-03

33.42 ± 2.65

(3.15 ± 1.08) E+ 03

(1.06 ± 0.12)

E-03

512.40 ± 191.31

  1. Values represent mean ± SEM of 3 to 5 independent experiments. Kinetic parameters were determined from the association phase (1 to 120 s) and dissociation phase (120 to 300 s) of the SPR sensorgrams. The apparent KD was calculated from the ratio of koff over kon (nM) determined by the 1:1 binding model with mass transfer correction. kon association rate constant (M−1 s−1); koff dissociation rate constant (s−1); KD dissociation equilibrium (affinity) constant
  2. N.D. not determined