Native membranes and Triton X-100 solubilized integral membrane proteins of peroxisomes from rat liver were reconstituted in liposomes. With the patch clamp technique, a channel was detected with a conductance of 420 +/- 30 pS and a PK/PC1 of about 3. The channel in native membrane fractions was weakly voltage dependent, residing most of the time in an open state with the possibility to shift to different substates. Solubilization changed the kinetic properties. The channel became strongly voltage dependent and closed at voltages negative to -20 mV. The estimated diameter of the channel is about 1.7 nm and might explain, at least partially, the permeability properties of the peroxisomal membrane.