Table 1.

Binding affinities of mouse TGF-β2 variants for BG_ZP-C and BG_O

All measurements, with the exception of those indicated in footnotes a and d, were made in HBS-EP buffer at pH 7.4 with TGF-βs minimally carboxy-biotinylated and captured on a high-density streptavidin surface.

TGF-β2 variant	BGZP-C binding		BGO binding
	Kd	Rmax	Kd	Rmax
	μm	RU	μm	RU
TGF-β2 WT	0.20 ± 0.12	315 ± 6	0.085 ± 0.023	398 ± 6
TGF-β2 WTa	0.611 ± 0.06	148 ± 5	NDb	NDb
TGF-β2 I33A	8.22 ± 0.14	250c	0.076 ± 0.001	315 ± 4
TGF-β2 E84A	0.17 ± 0.01	274 ± 4	0.065 ± 0.007	426 ± 5
TGF-β2 T87A	0.26 ± 0.01	268 ± 2	0.060 ± 0.001	379 ± 3
TGF-β2 L89A	0.27 ± 0.02	236 ± 5	0.083 ± 0.007	350 ± 10
TGF-β2 Y91A	0.40 ± 0.02	86 ± 2	0.22 ± 0.04	189 ± 9
TGF-β2 I92A	1.8 ± 0.2	159 ± 8	0.080 ± 0.01	286 ± 6
TGF-β2 I92D	12.6 ± 0.3	98c	0.36 ± 0.03	129 ± 4
TGF-β2 K97A	0.96 ± 0.07	110 ± 4	0.065 ± 0.001	182 ± 3
TGF-β2 K97V	1.97 ± 0.02	78c	0.11 ± 0.01	103 ± 3
TGF-β2 I98A	0.32 ± 0.02	267 ± 6	0.14 ± 0.01	336 ± 8
TGF-β2 E99A	1.5 ± 0.1	297 ± 12	0.12 ± 0.01	411 ± 12
TGF-β2 E99R	8.8 ± 0.6	79c	0.31 ± 0.07	114 ± 9
avi-mmTGF-β2–7 md	2.1 ± 0.1	76 ± 1	NDb	NDb

^a This was measured in 25 mm glycine, 150 mm NaCl, pH 11.0, with minimally carboxy-biotinylated TGF-β2 WT captured on a high-density streptavidin surface.

^b ND means not determined.

^cR_max value was constrained to the value shown based on the R_max obtained for binding of BG_O.

^d This was measured in HBS-EP buffer at pH 7.4 with biotinylated avi-tagged mmTGF-β2–7 m captured on a high-density streptavidin surface.