ISOLATION AND CHARACTERIZATION OF A PROTEINACEOUS INHIBITOR OF MICROBIAL PROTEINASES INDUCED DURING THE HYPERSENSITIVE REACTION OF TOBACCO TO TOBACCO MOSAIC-VIRUS

被引：63

作者：

GEOFFROY, P ^{[1
]}

LEGRAND, M ^{[1
]}

FRITIG, B ^{[1
]}

机构：

[1] UNIV STRASBOURG 1,CNRS,INST BIOL MOLEC,RUE GEN ZIMMER 12,F-67070 STRASBOURG,FRANCE

来源：

MOLECULAR PLANT-MICROBE INTERACTIONS | 1990年 / 3卷 / 05期

关键词：

Antibodies; Purification to homogeneity; Specificity;

D O I：

10.1094/MPMI-3-327

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 proteinase inhibitor is strongly induced in tobacco leaves reacting hypersensitively to tobacco mosaic virus. The tobacco inhibitor is highly active against four different serine endo-proteinases of fungal and bacterial origin (EC 3.4.21.14) but inhibits poorly two serine endoproteinases of animal origin, trypsin (EC 3.4.21.4) and chymotrypsin (EC 3.4.21.1). The inhibitor has been purified to homogeneity by successive steps of conventional and high-performance liquid chromatography. When electrophoresed under denaturing conditions, it behaves as a small polypeptide with a molecular weight of about 6,000. From its amino acid composition and NH2-terminal amino acid sequence analysis, it appears that the inhibitor belongs to the potato inhibitor I family. A polyclonal antiserum was raised against the purified tobacco inhibitor and was used in immuno-blotting experiments to follow inhibitor accumulation during the hypersensitive reaction of tobacco to tobacco mosaic virus. The inhibitor is highly efficient and might represent a potent fungicide and/or bactericide to be used in plant biotechnology. © 1990 The American Phytopathological Society.

引用

页码：327 / 333

页数：7

共 40 条

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