The present investigation addresses the mode of inhibition of the camel retinal acetylcholinesterase (AChE) activity by gallamine triethiodide, which is known to be a specific non-depolarizing neuromuscular blocking agent and polar cholinergic antagonist. This study gave the following results: it was found that gallamine (GA) reversibly inhibited the AChE activity in a concentration dependent manner, the IC 5 0 being about 0.633 mM. The K m for the hydrolysis of acetylthiocholine iodide by AChE was found to be 0.0803 mM in the control system, and the value increased by 19-463% in the GA (0.125-1.0 mM) treated systems. The V m a x was 0.649 μmol/min per mg protein for the control as well as GA treated systems. Dixon as well as Lineweaver-Burk plots and their secondary replots indicated that the nature of the inhibition is of the reversible competitive type. The K i value was estimated as 0.160 mM. TheK i value increased with an increase in substrate concentration. The turnover number (K c a t ) and specificity constant (K s p ) were 62.1 min - 1 and 7.73 10 5 (M min) - 1 in the control system while the value for one parameter (K s p ) was decreased by 25-83% in the GA (0.125-1.0 mM) treated systems.