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. 2007 Jul 10;97(3):315–321. doi: 10.1038/sj.bjc.6603881

Table 3. Determination of kinetic constants for antibody-EpCAM interactions.

Antibody kass (M−1s−1) kdiss (s−1) KD (M)
HO-3 5.4±1.6 × 104 2.7±0.8 × 10−5 5.5 × 10−10±0.19
Catumaxomab 6.1±1.5 × 104 3.3±0.3 × 10−5 5.6 × 10−10±0.12

Interaction between the ECD of native EpCAM and mAb was measured by surface plasmon resonance. Both the parental mAb HO-3 and the trAb variant catumaxomab displayed high-affinity binding with slow off rates.