AFFINITY PURIFICATION OF HYDRA GLUTATHIONE BINDING-PROTEINS

The association of glutathione (GSH) with putative external chemorecep tors elicits feeding behavior in Hydra, In the present study, solubili zed membrane proteins were chromatographed on an affinity column of im mobilized GSH in order to isolate GSH-binding proteins that may repres ent the Xydra GSH chemoreceptor. The most abundant of the affinity-pur ified proteins was a triplet of peptides ranging in molecular weight f rom 24.5-26 kDa. Antiserum generated against the 24.5-26 kDa triplet p eptides inhibited GSH-stimulated feeding behavior by 47%, implicating a role for one or more of these peptides in Hydra chemoreception.