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- W2002245237 abstract "A theoretical relation between permeability and ionic concentrations in a bathing solution has been derived by assuming that only channels unoccupied by a competing non-permeable ion can transport ions specific for that channel. The affinities of the channel to the ion and the competitor are expressed by dissociation constants of the ion-site and competitor-site complexes in the channel. Analyses of the relation of K permeability to [K] o obtained from myelinated nerve fibres and Nitella cells revealed that the affinity of sites in K channels was independent of membrane potential, whereas K conductivity increased with depolarization. The value of the dissociation constant of the K + -site complex, K 1 , was estimated as 1244 m m for myelinated nerve, and K 1 exp(ψ 0 F RT ) for Nitella was 17.5 m m ( ψ 0 is the surface potential at the outer surface of membrane). The dependence on voltage of the total number of K channels was estimated from the dependence of K conductance on membrane potential at [K] o = [K] 1 (obtained from the theoretical magnitude of K current computed by using the dissociation constants described above). It should be noted that when the channels are partially saturated with K + , neither the chord conductance nor the “permeability coefficient”, as defined in the Goldman and Hodgkin-Katz formulation, correctly represents the dependence on membrane potential of the total number of channels." @default.
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- W2002245237 date "1975-05-01" @default.
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- W2002245237 title "An analysis of the change in K-permeability on depolarization in terms of affinity and numbers of total channels" @default.
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- W2002245237 doi "https://doi.org/10.1016/0022-5193(75)90147-2" @default.
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