Affinity purification of Hydra glutathione binding proteins
Document Type
Article
Date of Original Version
11-14-1994
Abstract
The association of glutathione (GSH) with putative external chemoreceptors elicits feeding behavior in Hydra. In the present study, solubilized membrane proteins were chromatographed on an affinity column of immobilized GSH in order to isolate GSH-binding proteins that may represent the Hydra GSH chemoreceptor. The most abundant of the affinity-purified proteins was a triplet of peptides ranging in molecular weight from 24.5-26 kDa. Antiserum generated against the 24.5-26 kDa triplet peptides inhibited GSH-stimulated feeding behavior by 47%, implicating a role for one or more of these peptides in Hydra chemoreception. © 1994.
Publication Title, e.g., Journal
FEBS Letters
Volume
354
Issue
3
Citation/Publisher Attribution
Bellis, Susan L., David C. Laux, and Dennis E. E. Rhoads. "Affinity purification of Hydra glutathione binding proteins." FEBS Letters 354, 3 (1994): 320-324. doi: 10.1016/0014-5793(94)01154-0.