Affinity purification of Hydra glutathione binding proteins

Authors

Susan L. Bellis, University of Rhode Island
David C. Laux, University of Rhode Island
Dennis E. E. Rhoads, University of Rhode Island

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.