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Table 1 Thermodynamic properties and surface mass density of IC formation obtained by SE using VLPs and mAbs of different clones

From: Structural properties of immune complexes formed by viral antigens and specific antibodies shape the inflammatory response of macrophages

ΓSE, ng/cm2

ka, M–1 s–1

kd, s–1

kr, s–1

KA, M–1

KD, M

WUPyV VLP

 392

–

–

–

–

–

IgG1 mAb (clone 11D2)

 51.3

1.76 · 104

2.21 · 10–4

1.97 · 10–5

7.96 · 108

1.26 · 10–9

IgG2a mAb (clone 12F8)

 44.9

8.80 · 103

6.18 · 10–7

1.78 · 10–7

1.43 · 1010

7.01 · 10–11

IgG2a mAb (clone 4E12)

 28.4

2.48 · 104

1.40 · 10–5

6.40 · 10–6

1.77 · 109

5.64 · 10–10

IgG2b mAb (clone 5H10)

 60.9

1.27 · 104

1.42 · 10–6

1.56 · 10–6

8.93 · 109

1.12 · 10–10

  1. ΓSE dry protein surface mass density, ka association rate constant, kd dissociation rate constant, kr the stable immune complex formation rate constant, KA the equilibrium association constant, and KD dissociation constant
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Cell & Bioscience

ISSN: 2045-3701

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