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. Author manuscript; available in PMC: 2017 Feb 1.
Published in final edited form as: J Pharm Sci. 2016 Jan 9;105(2):559–574. doi: 10.1016/j.xphs.2015.11.003

Table 1.

Kinetic parameters obtained for binding of FcγRIIIa with IgG1 Fc glycoforms. Binding kinetics were measured at 25°C. The data shows kinetic association rate ka, kinetic dissociation rate kd, and equilibrium dissociation constant KD. These data are averaged values of six independent experiments.

Glycoforms Immobilized
protein		 Immobilization
technique		 Average ka × 10−5
(1/Ms)		 Average kd × 103
(1/s)		 Average KD
(nM)
HM-Fc IgG1 Fc Protein G 1.9 ± 0.3 5.4 ± 1.0 27.7 ± 6.4
FcγRIIIa Streptavidin 3.0 ± 0.6 7.9 ± 1.4 26.4 ± 6.9
Man5-Fc IgG1 Fc Protein G 1.6 ± 0.1 5.1 ± 0.9 31.8 ± 5.9
FcγRIIIa Streptavidin 2.2 ± 0.2 7.3 ± 0.3 32.8 ± 3.1
GlcNAc-Fc IgG1 Fc Protein G 1.2 ± 0.2 140.0 ± 9.1 1115.0 ± 136.8
FcγRIIIa Streptavidin 1.6 ± 0.3 161.3 ± 21.8 995.0 ± 219.3
N297Q-Fc IgG1 Fc / FcγRIIIa Protein G / Streptavidin * * *
*

For N297Q, there was no detectable binding at the highest concentration tested (20 µM) for both methods.