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. 2004 Aug 24;382(Pt 2):677–685. doi: 10.1042/BJ20040358

Table 3. Kinetic parameters for the interaction of the full-length ankyrin-binding domain and its mutants with PE/PC mono- and bi-layers obtained from SPR measurements (Figure 5) and pelleting assay (Figure 3).

The parameters were determined as described in the Materials and methods section. In addition, KD and Rmax values for the interaction of the full-length ankyrin-binding domain and Frag.5 with the hydrophobic surface of a bare chip (hexadecane thiol-covered) are presented.

Pelleting assay (Figure 3) SPR (PE/PC) (Figure 5) Hydrophobic surface
Protein KD (μM]) Bmax (μg/mg of phospholipid) KD (μM) Rmax KD (μM) Rmax
DWA 0.05 3.81 0.27 124 0.449 127
N1C 0.107 3.62 0.234 119
FRAG.1 0.25 5.57 0.363 124
FRAG.3 0.18 11.9 0.25 978
FRAG.5 0.79 38.8 0.18 516 27.8 6910