AFFINITY PURIFICATION OF HYDRA GLUTATHIONE BINDING-PROTEINS

被引：12

作者：

BELLIS, SL ^{[1
]}

LAUX, DC ^{[1
]}

RHOADS, DE ^{[1
]}

机构：

[1] UNIV RHODE ISL, DEPT MOLEC GENET BIOCHEM & MICROBIOL, KINGSTON, RI 02881 USA

来源：

FEBS LETTERS | 1994年 / 354卷 / 03期

关键词：

HYDRA; COELENTERATE; GLUTATHIONE; CHEMORECEPTOR; FEEDING BEHAVIOR;

D O I：

10.1016/0014-5793(94)01154-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 Xydra 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.

引用

页码：320 / 324

页数：5

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