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Sterile detached barley leaves were floated on water or kinetin (10 mg/1)and supernatant extracts (30,000 x g for 30 min) were prepared from these leaves over an 8 day incubation period. Changes in selected total enzyme levels and in individual soluble protein components wore compared. Ribonuclease, deoxyribonuclease and peptidase activities rose in senescing leaves, even as total protein levels fell. Kinetin to some extent depressed these activities. Evidence of considerable loss of ribonuclease and to a lesser extent of deoxyribonuclease into the surrounding medium was obtained. Soluble supernatant ant extracts were resolved on DEAE‐Sephadex (A‐50) columns into about 15 components. While most components were degraded during senescence they did so at different rates. Kinetin lowered the rate of degradation of all components. Since no conclusive evidence of a new protein(s) was obtained in water and kinetin treated leaves, it was considered that any protein changes may have been of a quantitative rather than qualitative nature.
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Atkin et al. (1969) studied this question.
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