Characterization of a highly stable trypsin-like proteinase inhibitor from the seeds of Opuntia streptacantha (O. streptacantha Lemaire)

被引：17

作者：

Torres-Castillo, J. A. ^{[1
]}

Mondragon Jacobo, C. ^{[2
]}

Blanco-Labra, A. ^{[1
]}

机构：

[1] IPN, Ctr Invest & Estudios Avanzados, Unidad Irapuato, Irapuato 36821, Gto, Mexico

[2] CE Bajio INIFAP, Celaya S M Allende, Gto, Mexico

来源：

PHYTOCHEMISTRY | 2009年 / 70卷 / 11-12期

关键词：

Opuntia streptacantha; Cactaceae; Prickly pear; Proteinase inhibitor; Seed protein; Trypsin inhibitor; Insect resistance; SERINE-PROTEASE INHIBITOR; MOLECULAR EVOLUTION; POLYMORPHISM; CONSERVATION; DIVERSITY; L;

D O I：

10.1016/j.phytochem.2009.08.009

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：

A trypsin inhibitor from Opuntia streptacantha Lemaire (Prickly pear) seeds was purified and characterized. Of several proteases tested, this inhibitor showed specificity to trypsin-like enzymes. The major inhibitor present in these seeds showed distinctive characteristics, most notably a low molecular weight of 4.19 kDa, as determined by MALDI TOF, and an unusually high thermal stability, retaining most of the activity after heating the sample 1 h to 120 degrees C with a pressure of 1 kg/cm(2). Its complete amino acid sequence was obtained through mass spectrometry, this establishing presence a blocked N-terminal region. When comparing its sequence in the MEROPS database for peptidases and peptidase inhibitors, it showed 34.48% identity with a serine-proteinase inhibitor from the 115 family. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：1374 / 1381

页数：8

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