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来自欧芹(Petroselinum crispum)的一种寡肽激发子受体的特性鉴定与部分纯化。

Characterization and partial purification of an oligopeptide elicitor receptor from parsley (Petroselinum crispum).

作者信息

Nennstiel D, Scheel D, Nürnberger T

机构信息

Institut für Pflanzenbiochemie, Abteilung Stress- und Entwicklungsbiologie, Halle/Saale, Germany.

出版信息

FEBS Lett. 1998 Jul 24;431(3):405-10. doi: 10.1016/s0014-5793(98)00800-x.

DOI:10.1016/s0014-5793(98)00800-x
PMID:9714552
Abstract

Parsley cells recognize the fungal phytopathogen Phytophthora sojae through a plasma membrane receptor. A 13 amino acid oligopeptide fragment (Pep-13) of a 42 kDa fungal cell wall glycoprotein was shown to bind to the receptor and stimulate a complex defense response in cultured parsley cells. The Pep-13 binding site solubilized from parsley microsomal membranes by non-ionic detergents exhibited the same ligand affinity and ligand specificity as the membrane-bound receptor. Chemical crosslinking and photoaffinity labeling assays with [125I]Pep-13 revealed that a monomeric 100 kDa integral plasma membrane protein is sufficient for ligand binding and may thus constitute the ligand binding domain of the receptor. Ligand affinity chromatography of solubilized microsomal membrane protein on immobilized Pep-13 yielded a 5000-fold enrichment of specific receptor activity.

摘要

芹菜细胞通过质膜受体识别真菌植物病原体大豆疫霉。一种42 kDa真菌细胞壁糖蛋白的13个氨基酸的寡肽片段(Pep - 13)被证明能与该受体结合,并在培养的芹菜细胞中刺激复杂的防御反应。用非离子去污剂从芹菜微粒体膜中溶解出来的Pep - 13结合位点表现出与膜结合受体相同的配体亲和力和配体特异性。用[125I]Pep - 13进行的化学交联和光亲和标记试验表明,一种单体的100 kDa整合质膜蛋白足以进行配体结合,因此可能构成受体的配体结合结构域。在固定化的Pep - 13上对溶解的微粒体膜蛋白进行配体亲和层析,使特异性受体活性富集了5000倍。

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Characterization and partial purification of an oligopeptide elicitor receptor from parsley (Petroselinum crispum).来自欧芹(Petroselinum crispum)的一种寡肽激发子受体的特性鉴定与部分纯化。
FEBS Lett. 1998 Jul 24;431(3):405-10. doi: 10.1016/s0014-5793(98)00800-x.
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