Trypsin-sensitive, rapid inactivation of calcium-activated potassium channel

Christopher R. Solaro, Christopher J. Lingle

Research output: Contribution to journalArticlepeer-review

93 Scopus citations


Most calcium-activated potassium channels couple changes in intracellular calcium to membrane excitability by conducting a current with a probability that depends directly on submembrane calcium concentration. In rat adrenal chromaffin cells, however, a large conductance, voltage- and calcium-activated potassium channel (BK) undergoes rapid inactivation, suggesting that this channel has a physiological role different than that of other BK channels. The inactivation of the BK channel, like that of the voltage-gated Shaker B potassium channel, is removed by trypsin digestion and channels are blocked by the Shaker B amino-terminal inactivating domain. Thus, this BK channel shares functional and possibly structural homologies with other inactivating voltage-gated potassium channels.

Original languageEnglish
Pages (from-to)1694-1698
Number of pages5
Issue number5077
StatePublished - 1992


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