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Properties of inhibitors of plant virus infection occurring in the leaves of species in the Chenopodiales
Author(s) -
SMOOKLER M. M.
Publication year - 1971
Publication title -
annals of applied biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.677
H-Index - 80
eISSN - 1744-7348
pISSN - 0003-4746
DOI - 10.1111/j.1744-7348.1971.tb04668.x
Subject(s) - chenopodium , biology , chenopodium quinoa , chenopodiaceae , sephadex , phaseolus , size exclusion chromatography , botany , chromatography , biochemistry , enzyme , chemistry , weed
SUMMARY Leaf extracts from twenty‐nine species of the Chenopodiales were shown to inhibit the infection of Phaseolus vulgaris by tobacco necrosis virus. The inhibitors were not lost on dialysis or by storage at ‐ 25 d̀C for 56 days. Partially dry lyophilized extracts kept at ‐ 25 d̀C for 2 years in unsealed screwtopped bottles retained inhibitory activity. The inhibitors in extracts of species of Beta, Halimione and Amaranthus were largely inactivated by heating for 10 min at 60–80 d̀C, but 80–100 d̀C was needed to inactivate those in sap of species of Chenopodium, Atriplex, Basella, Hablitzia, Salsola and Celosia . The extent of this inhibition of infection caused by unheated Chenopodium album sap depended on the virus‐host combination. With heated sap this dependence was changed. The properties of inhibitors from extracts of Chenopodium amaranticolor, C. album, Atriplex nitens and Amaranthus caudatus were compared. Extracts made with water‐saturated phenol were not inhibitory and precipitation tests with 50% acetone, 50% ethanol and 2.5% trichloracetic acid suggested that the inhibitors are protein. Most inhibitory activity was precipitated from extracts by 70–90% saturated ammonium sulphate. Ion‐exchange column chromatography on CM‐Sephadex C‐25 showed that most inhibitory activity and protein was eluted by 0.4 M sodium acetate buffer. Disc electrophoresis indicated that several proteins occurred within the pooled inhibitory fractions. Gel filtration with Sephadex G‐200 suggested that the inhibitors have molecular weights of 25000–38000. The four inhibitors are probably very similar, but not necessarily identical, basic proteins.