Soluble acid invertases, obtained from the developing third leaf of oat, were fractionated by gel filtration and ion-exchange chromatography. Gel filtration separated two peaks. Isoenzyme II (85 × 103 daltons) was the dominant form in the non-emerged leaf but decreased in activity after leaf emergence. The activity of isoenzyme I (143 × 103 daltons) remained constant throughout leaf development and was dominant in mature tissues. Ion-exchange chromatography separated two discrete peaks (A and B) and a composite peak (C), comprised several isoenzymes. The activities associated with A, B and C varied considerably during leaf development. One or more of the isoenzymes of invertase in peak C was the predominant invertase at all stages of leaf development. These observations are discussed in relation to the role and control of synthesis of invertases during development.
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