Aleurone grains were extracted from peanut cotyledons and purified on a sucrose density gradient. The protein isolated from this organelle appeared to be of a single macromolecular weight. Its purity was tested by gel filtration and disc electrophoresis. Exposure to 0·5 and 1 Mrad of this isolated buffer-suspended protein resulted in a breakdown of the molecules as was demonstrated by their multiple elution peaks on Sephadex G25 following exposure. The amount of small molecular fragments formed increased with a higher dose. The proteolytic activity was greatly suppressed following irradiation. © 1971.
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