Changes in Barley Leaf Ribonucleases During Early Stages of Infection byErysiphe graminisf. sp.hordei

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Abstract
RNase fractions from the barley powdery mildew fungus (E. graminis f. sp. hordei Marchal, race 3) and a susceptible cultivar of barley (Hordeum vulgare ''Prior'') were purified to a high specific activity by Sephadex G-100 gel filtration in the presence of 3.0 M urea. Upon gel filtration the enzymes (termed pH 5-insoluble RNases of MW 24,000 and 10,000, respectively) from healthy and inoculated plants yield 2 distinct peaks of enzymatic activity. The corresonding enzyme fraction from the powdery mildew fungus yields a single peak of activity of MW about 12,000 daltons. The major peak of RNase activity obtained from inoculated barley leaves 48 h after inoculation is remarkably different from that obtained from the healthy leaves or from the fungus with respect to its substrate preference as judged by the relative rates of hydrolysis of synthetic ribohomopolymers. These results suggest a dramatic change in the catalytic properties of this RNase of barley leaves at an early stage of host-parasite interactions.

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