Assay for Helminthosporium maydis Toxin-binding Activity in Plants.
نویسندگان
چکیده
A relatively rapid and sensitive assay is described for assessing the binding of Helminthosporium maydis Race T(14) C-toxins I and II to plant components. The technique is a modification of the one of Haddad and Birge (J. Biol. Chem. 250: 299-303, 1975), and utilizes dextran-coated charcoal as an adsorbent for the unreacted toxin and employs a Millipore filter to isolate the protein-toxin complex.Extracts from susceptible corn line W64A Tms possess a protein primarily localized in the cytosol which is relatively heat-insensitive, ficin- and papain-sensitive, and binds toxins I and II at half-saturation in the order of 0.1 mm. The toxin-binding activities of the extracts of various corn lines and other species are not correlated to resistance or susceptibility to H. maydis Race T, nor to sensitivity to the toxins. These findings are discussed relative to the function of the binding protein and cellular sensitivity to the toxins.
منابع مشابه
The Toxins of Helminthosporium maydis (Race T) : A Colorimetric Determination of the Toxins, Their Appearance in Culture and in Infected Plants.
Host-specific toxins produced by Helminthosporium maydis, race T, are measured quantitatively by a chemical assay procedure involving reaction of the toxins with a sulfuric acidacetic anhydride reagent and measurement of the absorbance of the product at 330 nm. The assay was shown to measure total toxin concentrations after only limited fractionation of the culture medium. Using the assay it wa...
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A toxin preparation from Helminthosporium maydis Race T containing several closely related molecules with apparently identical biological activities was highly active against mitochondria and protoplasts from Texas male-sterile (T) cytoplasm corn (T mitochondria and T protoplasts, respectively) but had no effect on their male-fertile (N) cytoplasm counterparts. The toxin preparation caused mult...
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The mechanism by which Helminthosporium maydis race T toxin inhibits respiration dependent on NAD(+)-linked substrates in T cytoplasm corn mitochondria was investigated. The toxin did not cause leakage of the soluble matrix enzyme malate dehydrogenase from the mitochondria or inhibit malate dehydrogenase or isocitrate dehydrogenase directly. The toxin did increase the permeability of the inner ...
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ورودعنوان ژورنال:
- Plant physiology
دوره 60 1 شماره
صفحات -
تاریخ انتشار 1977