Reactivation efficacy of methoxime (MMB-4) and its homologues with increasing length of the alkylene bridge between the pyridinium rings up to the sixth member of the series has been studied in reactivation of AChE, inhibited by sarin, cyclosarin and soman. The efficacy was evaluated using AChE, immobilized and stabilized on a cotton fabric, and an indicator paper with acetylthiocholine iodide as substrate and 5,5´‑dithiobis(2‑nitrobenzoic acid) as chromogenic agent. The activity of AChE was determined by measurement of remission changes of the fabric surface. After treatment of AChE-sarin complex for 10 minutes, the reactivation efficacy of the first three members of the homologous series is comparable. With reactivation time prolonged to 15 minutes, TMB-4 becomes the most potent reactivator, especially at lower reactivator concentrations. Further extension of the bridge between the pyridinium nuclei results in decrease of the reactivation efficacy. With AChE, inhibited by cyclosarin and soman, only MMB-4 showed some effect; lower reactivation values being generally found for the soman-inhibited enzyme.