TABLE 1.

Binding parameters from ELISA PI(4,5)P2 experiments

The maximal binding, B_max, is reported in arbitrary units. The dissociation constant, k_d, is reported in nm. Data are the mean ± S.D. from 3 (KR/A) and 6 (WT, AXXA3, RXXR3) independent experiments. ND, not determined.

Construct	Bmax		kd
	pH 7.5	pH 7.0	pH 7.5	pH 7.0
Wild type	0.87 ± 0.04	1.00 ± 0.04a	65 ± 10	38 ± 6a
AXXA3	0.76 ± 0.04b	0.79 ± 0.03c	78 ± 14	62 ± 9c
RXXR3	0.97 ± 0.05	0.97 ± 0.03	67 ± 13	44 ± 5
KR/A	0.16 ± 0.04d	0.27 ± 0.01d,e	ND	ND

^a p < 0.05 compared to pH 7.5.

^b p < 0.05 compared to WT and RXXR3 at pH 7.5.

^c p < 0.05 compared to WT and RXXR3 at pH 7.0.

^d p < 0.01 compared to WT.

^e p < 0.001 compared to pH 7.5.