Purification and partial characterization of antiviral proteins from Chenopodium album L. leaves

被引：6

作者：

Dutt, S ^{[1
]}

Balasubrahmanyam, A ^{[1
]}

Lodha, ML ^{[1
]}

机构：

[1] Indian Agr Res Inst, Div Biochem, New Delhi 110012, India

来源：

JOURNAL OF PLANT PHYSIOLOGY | 2000年 / 156卷 / 5-6期

关键词：

Chenopodium album; antiviral proteins; purification;

D O I：

10.1016/S0176-1617(00)80253-9

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Two antiviral proteins from leaves of Chenopodium album L, have been purified and their characteristics compared. Both of these impart resistance in hypersensitive hosts: against tobacco mosaic virus in Nicotiana tabacum cv. Samsun NN and N. glutinosa, and sunnhemp rosette virus in Cyamopsis tetragonoloba. One of them exhibited a single polypeptide with a molecular mass of 25 kD, and the other one is a complex showing polypeptide bands of 27, 25 and 18kD on SDS-PAGE. The 25 kD protein and the complex protein inhibited more than 90 % lesion formation at a concentration of 20-22 mu g mL(-1). Both of the proteins are basic in nature and can tolerate high temperature (up to 90 degrees C).

引用

页码：808 / 810

页数：3

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