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Purification and characterization of a unique, potent, peptidyl probe for the high conductance calcium-activated potassium channel from venom of the scorpion Buthus tamulus.
Data suggest that IbTX interacts at a distinct site on the channel and modulates ChTX binding by an allosteric mechanism, which defines a new class of peptidyl inhibitor of PK,Ca with unique properties that make it useful for investigating the characteristics of this channel in target tissues.
Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom.
Three new toxins from the venom of the scorpion Leiurus quinquestriatus var. hebraeus have been identified on the basis of their ability to block the Shaker K+ channel. These toxins have been
Distribution of high-conductance Ca(2+)-activated K+ channels in rat brain: targeting to axons and nerve terminals
The expression pattern of Slo is consistent with its targeting into a presynaptic compartment, which implies an important role in neural transmission.
Purification, characterization, and biosynthesis of margatoxin, a component of Centruroides margaritatus venom that selectively inhibits voltage-dependent potassium channels.
A novel peptidyl inhibitor of K+ channels has been purified to homogeneity from venom of the new world scorpion Centruroides margaritatus and displays significant sequence homology with previously identified K+ channel inhibitors.
Mode of action of iberiotoxin, a potent blocker of the large conductance Ca(2+)-activated K+ channel.
From single-channel records it was possible to determine that iberiotoxin binds to Ca(2+)-activate K+ channel in a bimolecular reaction indicating that the surface charges located in the external channel vestibule play an important role in modulating toxin binding.
Primary sequence and immunological characterization of beta-subunit of high conductance Ca(2+)-activated K+ channel from smooth muscle.
The data demonstrate that, in vivo, the high conductance Ca(2+)-activated K+ channel exists as a multimer containing both alpha- andbeta-subunits, and this cDNA represents the first beta-subunit of a potassium channel cloned to date.
Subunit composition of the high conductance calcium-activated potassium channel from smooth muscle, a representative of the mSlo and slowpoke family of potassium channels.
The results indicate that the alpha-sub unit of the purified tracheal smooth muscle maxi-K channel is a member of the mSlo family of K+ channels and forms a noncovalent complex with a beta-subunit.
Mechanism of iberiotoxin block of the large-conductance calcium-activated potassium channel from bovine aortic smooth muscle.
The interaction of iberiotoxin (IbTX) with the large-conductance calcium-activated potassium (maxi-K) channel was examined by measuring single-channel currents from maxo-K channels incorporated into planar lipid bilayers, suggesting that IbTX blocks the maxi-k channel through a simple bimolecular binding reaction where the silent periods represent times when a single toxin molecule is bound to the channel.
Complex Subunit Assembly of Neuronal Voltage-gated K+Channels
In vivo subunit coassembly provides the structural basis for toxin binding pharmacology and can lead to the association of as many as three distinct channel subunits to form functional K+channels in vivo.
Selective blockers of voltage-gated K+ channels depolarize human T lymphocytes: mechanism of the antiproliferative effect of charybdotoxin.
It is concluded that the membrane potential of resting T cells is set by voltage-activated channels and that blockade of these channels is sufficient to depolarize resting human T cells and prevent activation.