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Affinity purification of Hydra glutathione binding proteins
Author(s) -
Bellis Susan L.,
Laux David C.,
Rhoads Dennis E.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01154-0
Subject(s) - lernaean hydra , glutathione , chemistry , biochemistry , microbiology and biotechnology , biophysics , biology , enzyme
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.