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. 2015 Jan 8;25(6):591–606. doi: 10.1093/glycob/cwv001

Table II.

Kinetic data obtained from SPR analyses at pH 6.5

Construct KD (nM)
ka1 (M−1s−1 × 103)
kd1 (s−1 × 10−3)
Monoester
Diester
Monoester Diester Monoester Diester kd1/ka1 Steadystate kd1/ka1 Steadystate
D7–15 101 53 7.42 0.0706 74 97 1300 926
D14–15 6.4 4.6 0.11 0.14 17000 9600 29000 45000
KD2 (mM)
ka2 (M−1s−1 × 10−3)
kd2 (s−1 × 10−3)
kd2/ka2
Construct Monoester Diester Monoester Diester Monoester Diester
D7–15 0.69 7.1 0.13 5.7 0.19 0.81
D14–15 28 3.8 17.4 9.8 0.62 2.6

Kinetic and steady state affinity values determined from SPR sensorgrams obtained with GAA monoester and GAA diester immobilized on sensor chip surfaces. Purified recombinant protein was injected as the free analyte. Upper table reports kinetic parameters of the major component obtained from fitting sensorgrams to a two-state model with conformational change. The lower table reports kinetic parameters for the minor component with KD values reported in mM.