水螅谷胱甘肽结合蛋白的亲和纯化

Affinity purification of Hydra glutathione binding proteins.

作者信息

Bellis S L, Laux D C, Rhoads D E

机构信息

Department of Biochemistry, Microbiology and Molecular Genetics, University of Rhode Island, Kingston 02881.

出版信息

FEBS Lett. 1994 Nov 14;354(3):320-4. doi: 10.1016/0014-5793(94)01154-0.

DOI:10.1016/0014-5793(94)01154-0

PMID:7957948

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.

摘要

谷胱甘肽（GSH）与假定的外部化学感受器的结合引发了水螅的进食行为。在本研究中，将溶解的膜蛋白在固定化GSH的亲和柱上进行色谱分析，以分离可能代表水螅GSH化学感受器的GSH结合蛋白。亲和纯化的蛋白质中最丰富的是一组分子量在24.5 - 26 kDa之间的三联体肽。针对24.5 - 26 kDa三联体肽产生的抗血清使GSH刺激的进食行为受到47%的抑制，这表明这些肽中的一种或多种在水螅化学感受中发挥作用。