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. Author manuscript; available in PMC: 2015 Jan 14.
Published in final edited form as: Biochemistry. 2013 Dec 30;53(1):101–114. doi: 10.1021/bi4015133

TABLE 1.

CO Dissociation Constants for sGC Proteins

Protein α1 β1 KdCO (μM) KdCO′ (μM, +Ligand) Ref.
Bt sGC (full length) 1–691 1–619 127 ~26 YC-1 51
97 76
Hs sGC (full length) 1–690 1–619 260 77
Ms sGC-NT2 49–471 1–401 77 ± 7 1.7 ± 0.1 YC-1 33
90 ± 9 1.0 ± 0.1 YC-1 43
Ms sGC-NT13 49–450 1–380 2.8 ± 0.4 YC-1
53 ± 4 2.9 ± 0.2 PF-25 This work
0.25 ± 0.02a BAY
Ms sGC-NT19 49–450 1–380 50 ± 3 0.8 ± 0.1 YC-1 43
Ms sGC-NT21 272–450 1–380 0.20 ± 0.02a YC-1
2.2 ± 0.2a 0.24 ± 0.01a PF-25 This work
0.07 ± 0.01a BAY
Ms sGC β1(1–380) absent 1–380 0.20 ± 0.03a 0.18 ± 0.05a YC-1 This work
Bt sGC β1(1–197) absent 1–197 1.6 ± 0.2b 1.2 ± 0.2b YC-1 This work
Bt sGC β1(1–359) absent 1–359 15 ± 4 10 ± 3 YC-1 This work

Titration binding data were measured using gas-tight syringes and 1 or 10 cm cuvettes fitted with rubber septum. Protein concentration was 1 μM unless otherwise indicated. Where included for measuring KdCO′, the YC-1 and PF-25 concentrations were 50 μM, and BAY 41-2272 concentrations were 2.5 μM (Ms sGC-NT21) or 10 μM (Ms sGC-NT13). The values listed are the mean and standard deviation of at least three independent measurements.

a

Measured in a 10 cm cuvette, using 0.1 μM protein.

b

Measured in a 1 cm cuvette, using 0.5 μM protein.