TRANSLOCATION FROM LEAVES OF BARLEY INFECTED WITH BROWN RUST
نویسندگان
چکیده
منابع مشابه
Proteins in intercellular washing fluid from noninoculated and rust-affected leaves of wheat and barley.
Proteins in intercellular washing fluid (IWF) from wheat (Triticum aestivum) and barley (Hordeum vulgare) leaves were separated by two-dimensional isoelectric focusing-polyacrylamide gel electrophoresis and stained with Coomassie brilliant blue (CBB) or silver. Intracellular protein from the cut ends of leaves accounted for only a small proportion of total protein in IWF from wheat leaves. When...
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The barley leaf rust fungus forms appressoria over host leaf stomata and penetrates via the stomatal pore. High levels of avoidance to leaf rust fungi have been described in some wild accessions of Hordeum species where a prominent wax layer on the stomata inhibits triggering of fungal appressorium differentiation. Leaf rust avoidance has not yet been found in H. vulgare. Since cuticular leaf w...
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Nicotinamide nucleotide coenzymes were estimated spectrophotometrically in noninfected barley leaves and leaves infected with Erysiphe graminis var hordei (powdery mildew). Amounts of NADH, NADP(+) and NADPH were not altered by infection. In contrast, the NAD(+) content rose sharply and at 144 hours was 100% greater than in noninfected leaves. The respiratory rate was increased in infected leav...
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The barley leaf rust has been important in recent years in Iran. In order to identify the genetic resources of resistance to this disease, 207 Iranian barley landraces were studied. The germplasms were investigated at the field of Iraqi-Mahalleh research station in Gorgan as the disease hotspot under natural incidence over three years. The results showed that four genotypes including KC18638 an...
متن کاملPartial purification and characterization of endoproteinases from senescing barley leaves.
Two major endoproteinases were purified from senescing primary barley leaves. The major enzyme (EP(1)) appeared to be a thiol proteinase and accounted for about 85% of the total proteolytic activity measured in vitro. This proteinase was purified 5,800-fold and had a molecular weight of 28,300. It was highly unstable in the absence of dithiothreitol or at a pH greater than 7.5. Leupeptin, at a ...
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ژورنال
عنوان ژورنال: New Phytologist
سال: 1983
ISSN: 0028-646X,1469-8137
DOI: 10.1111/j.1469-8137.1983.tb02727.x