Prokaryotic channels, such as ELIC and GLIC, give key structural information for the Cys-loop superfamily. ELIC, a cationic channel from Erwinia chrisanthemi, is suitable also for single channel recording because of its high conductance (> 80 pS) (Zimmermann and Dutzler, 2011). Here we report on the kinetic properties of recombinant ELIC channels expressed in HEK293 cells. Single channel currents elicited by the full agonist propylamine (0.5-50 mM) were recorded from outside-out patches at -60 mV and analysed by maximum likelihood direct global fitting of kinetic schemes to the idealized data (HJCFIT program; Colquhoun et al 2003). Several mechanisms were tested and their adequacy was judged by comparing the predictions of the best fit obtained with the experimental open/shut time distributions and the dose response curve. The fitted model had to account also for the time course of macroscopic propylamine-activated currents, elicited by fast theta-tube applications (50-600 ms, 1-50 mM, -100 mV). Other Cys-loop channels, such as glycine receptors, activate via a pre-opening intermediate (‘flip’ model, Burzomato et al., 2004) and, when fully liganded, open with high efficacy to a single open state. In contrast with that, ELIC open time distributions at saturating propylamine showed more than one component. Thus, more than one open state must be accessible to the fully liganded channel. The `primed` model (Mukhtasimova et al., 2009) allows that by including more than one fully liganded intermediate. The best fit of this type of model showed that ELIC maximum open probability (99%) is reached when three molecules of agonist have bound to the channel. The overall efficacy of the fully liganded branch was 130 ± 20 (n = 3 sets; c.f. 20 for α1β glycine channels; Burzomato et al., 2004). The microscopic affinity for the agonist was seen to increase as the channel activated, from a resting state value of 6.2 ± 0.6 mM to 0.19 ± 0.11 mM (n = 3 sets) for the partially activated intermediate state. Macroscopic responses to propylamine had a monoexponential rising phase (time constant of 33 ± 4 ms at 10 mM, n= 16 patches), but a complex off-relaxation. This was notable for the presence of an almost instantaneous rebound current at the end of the application. The amplitude of this rebound current (normalized to the peak of the agonist current itself) increased with increasing propylamine concentration to reach 10% at 50 mM, but was voltage independent. We will present evidence that the rebound current is due to the relief of a low affinity, voltage-independent propylamine block of the open ELIC channel. The decay phase of the agonist currents (from the peak of the rebound current) appeared to be sigmoidal (e.g. two exponential components with amplitudes of opposite sign) and this time-course was well-described by the ‘primed’ mechanism fitted to the single channel records.