The Journal of Membrane Biology

, Volume 172, Issue 1, pp 37-45

First online:

A Component of Platypus (Ornithorhynchus anatinus) Venom Forms Slow-Kinetic Cation Channels

  • J.I.  KourieAffiliated withMembrane Transport Group, Department of Chemistry, The Faculties, The Australian National University, Canberra City, ACT, 0200 Australia

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The lipid bilayer technique is used to examine the biophysical properties of anion and cation channels frequently formed by platypus (Ornithorhynchus anatinus) venom (OaV). The OaV-formed anion channel in 250/50 mm KCl cis/trans has a maximum conductance of 857 ± 23 pS (n= 5) in 250/50 mm KCl cis/trans. The current-voltage relationship of this channel shows strong inward rectification. The channel activity undergoes time-dependent inactivation that can be removed by depolarizing voltage steps more positive than the reversal potential for chloride, E Cl , (+40 mV).

The reversal potential of the OaV-formed slow current activity in 250/50 mm KCl cis/trans is close to the potassium equilibrium potential (E K ) of −40 mV. The conductance values for the slow channel are 22.5 ± 2.6 pS and 41.38 ± 4.2 pS in 250/50 and 750/50 mm cis/trans, respectively. The gating kinetics of the slow ion channels are voltage-dependent. The channel open probability (P o ) is between 0.1 and 0.8 at potentials between 0 and +140 mV. The channel frequency (F o ) increases with depolarizing voltages between 0 and +140 mV, whereas mean open time (T o ) and mean closed time (T c ) decrease. Ion substitution experiments of the cis solution show that the channel has conductance values of 21.47 ± 2.3 and 0.53 ± 0.1 pS in 250 mm KCl and choline Cl, respectively. The amplitude of the single channel current is dependent on [K+] cis and the current reversal potential (E rev ) responds to increases in [K+] cis by shifting to more negative voltages. The increase in current amplitude as a function of increasing [K+] cis can be best described by a third order polynomial fit. At +140 mV, the values of the maximal single channel conductance (γ max ) and the concentration for half maximal γ (K s ) are 38.6 pS and 380 mm and decline to 15.76 pS and 250 mm at 0 mV, respectively. The ion selectivity of the channel to K+, Na+, Cs+ and choline+ was determined in ion substitution experiments. The permeability values for P K+ :P Na+ :P Cs+ :P choline+ were 1:1:0.63:0.089, respectively. On the other hand, the activity of the slow channel was eliminated (Fig. 7B). The slow channel was reversibly inhibited by [TEA+] trans and the half-maximal inhibitory concentration (K i ) was ∼48 mm.

Key words: Channel-forming peptides — Muscle relaxation — Fluid and electrolyte homeostasis — Edema — Pain — Signal transduction — Inward current