. Author manuscript; available in PMC: 2013 Dec 1.

Published in final edited form as: Mol Microbiol. 2012 Oct 24;86(5):1116–1131. doi: 10.1111/mmi.12045

Table 1.

Dissociation constants and kinetic data for various Fn- and dermatan sulfate-binding proteins interacting with Fn or dermatan sulfate, as determined by surface plasmon resonance.

Fn binding protein	Binding partners	K_on (10⁵s⁻¹M⁻¹)	K_off (s⁻¹)	K_D (μM)
RevA	Fn	1.71 ± 0.220	0.15 ± 0.023	0.88 ± 0.03
RevB	Fn	0.04 ± 0.015^a	0.11 ± 0.010^a	27.5 ± 6.14^a
BB0347	Fn	2.65 ± 0.492	0.16 ± 0.028	0.64 ± 0.02
BBK32	Fn	52.1 ± 2.1	0.10 ± 0.054	0.019 ± 0.009
BBK32	Dermatan sulfate	1.12 ± 0.115	0.02 ± 0.006	0.20 ± 0.03

Because the binding of RevB to Fn is weak, the determined values should be considered estimates.