Affinity purification of Hydra glutathione binding proteins

FEBS Letters

Rhoads, Dennis E.¹  Bellis, Susan L.¹  Laux, David C.¹ 

[1] Department of Biochemistry, Microbiology and Molecular Genetics, 117 Morrill Life Science Building, University of Rhode Island, Kingston, RI 02881, USA

关键词: Hydra;    Coelenterate;    Glutathione;    Chemoreceptor;    Feeding behavior;   

DOI  :  10.1016/0014-5793(94)01154-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown