Affinity purification of Hydra glutathione binding proteins.
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.
Department of Biochemistry, Microbiology and Molecular Genetics, University of Rhode Island, Kingston 02881.
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Bellis
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Laux
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Rhoads
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D002462:Cell Membrane / Q000737:chemistry; D002628:Chemoreceptor Cells / Q000378:metabolism*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005247:Feeding Behavior / Q000187:drug effects; D005978:Glutathione / Q000378:metabolism* / Q000494:pharmacology; D006829:Hydra / Q000737:chemistry*; D015151:Immunoblotting
D002352:Carrier Proteins; D005978:Glutathione