Current recordings from single chloride channels were obtained from excised and cell-attached patches of rat and human axons. In rat axons the channels showed an outwardly rectifying current-voltage relationship with a slope conductance of 33 pS at negative membrane potentials and 65 pS at positive potentials (symmetrical 150 mM CsC1). They were measurably permeable for cations (Ps,/Pcs/Pa = 0.1/0.2/1). Channel currents were independent of cytoplasmatic calcium concentration. Inactivation was not observed and gating was weakly voltage dependent. CI-channels in human axons showed similar gating behavior but had a lower conductance.Enzymatic dissociation and demyelination of myelinated axons enables single channel current recordings from the nodal and paranodal region [11]. Using this method one type of Na + channel and several types of K + channel have been described [11,12]. Another axonal conductance known from macroscopic current recordings in squid axons [10], non-myelinated rat axons [3] and myelinated rabbit axons [4] is CI-dependent. To our knowledge, single chloride channels have not been described previously in mammalian axons.A certain type of CI-channel with distinctive properties has been found in a variety of other cells, e.g. cultured hippocampal neurons [5,16], Drosophila neurons [18], crustacean axons [13] or tracheal epithelial cells [17]. This channel has an intermediate conductance (10-100 pS), is significantly permeable to cations (permeability ratio in the range of 0.1-0.35) and shows weak voltage-dependent gating. This type of channel has been designated as a 'background' CI-channel by Franciolini and Petris [6]. A C1-channel with similar electrophysiological characteristics was observed in about 5% of all gigaseal recordings from axonal patches obtained in the present study.Experiments were performed on ventral rat spinal roots and specimens of human sural nerves. Male Wistar rats (250-350 g) were anaesthetized with urethane (1.25 mg/kg, i.p.). After laminectomy 5 -10 ventral roots were removed and transferred into a culture dish. Enzymatic