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2,3-Butanedione monoxime (BDM) chemically removes phosphate groups from many proteins, and its action on DRK1 channels was examined after expression of DRK1 cRNA in Xenopus oocytes. In two-microelectrode voltage-clamp experiments, the application of 2,3-Butanedione monoxime to the bath inhibited DRK1 current (ki = 16.6 mM, H = 0.96) rapidly and reversibly, with a time course similar to the time course of solution change within the bath. DRK1 current was inhibited at all potentials; the time course of current activation, deactivation and inactivation were unaffected by 2,3-Butanedione monoxime. In inside-out patch-clamp experiments, the application of 2,3-Butanedione monoxime to the cytoplasmic surface similarly inhibited channel activity rapidly and reversibly (ki = 10.7 mM, H = 1.01) in the absence of rephosphorylating substrates. These results are inconsistent with a phosphatase effect, because such an effect should be irreversible in cell-free, ATP-free patches. Instead, the results suggest that 2,3-Butanedione monoxime can inhibit DRK1 channels directly from inside or outside of the membrane.
| Molecular Weight | 101.1 |
| Formula | C4H7NO2 |
| CAS Number | 57-71-6 |
| Solubility (25°C) | DMSO ≥ 30 mg/mL |
| Storage | 2-8°C, dry, sealed |
[3] Arthur Forer, et al. Does 2,3-butanedione monoxime inhibit nonmuscle myosin?
[5] L C Sellin, et al. Multiple effects of 2,3-butanedione monoxime
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