Complete amino acid sequence of puroindoline, a new basic and cystine‐rich protein with a unique tryptophan‐rich domain, isolated from wheat endosperm by Triton X‐114 phase partitioning

FEBS Letters

Blochet, Jean-Erik⁵  Joudrier, Philippe²  Chevalier, Catherine¹  Marion, Didier⁵  Forest, Eric⁴  Pézolet, Michel³  Pebay-Peyroula, Eva⁴  Gautier, Marie-Françoise² 

[1] Institut de Biologie, INSERM U211, 44035 Nantes Cédex 01, France;Laboratoire de Technologie des Céréales, INRA, 34060 Montpellier Cédex 01, France;CERSIM, Département de Chimie, Université Laval, Québec G1K 7P4, Canada;Institut de Biologie Structurale, 38047 Grenoble Cédex, France;Laboratoire de Biochimie et Technologie des Protéines, INRA, 44026 Nantes Cédex 03, France

关键词: Puroindoline;    Thionin;    Triton X-114;    Basic protein;    Cystine-rich protein;    Tryptophan;    nsLTP;    non-specific lipid transfer protein;    HPS;    hydrophobic protein of soja;    TX114;    Triton X-114;    EDTA;    ethylene-diamine-tetraacetic acid;    RP-HPLC;    reverse-phase high-performance liquid chromatography;    SDS;    sodium dodecyl sulfate;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(93)80249-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A new basic protein has been isolated from wheat endosperm by Triton X-114 phase partitioning. It contains five disulfide bridges and is composed of equal amounts of a polypeptide chain of 115 amino acid residues and of the same chain with a C-terminus dipeptide extension. The most striking sequence feature is the presence of a unique tryptophan-rich domain so that this protein isolated from wheat seeds has been named puroindoline. The similar phase partitioning behavior in Triton X-114 of this basic eystine-rich protein and of purothionins suggests that puroindoline may also be a membranotoxin that might play a role in the defense mechanism of plants against microbial pathogens.

【 授权许可】

Unknown