α-Amylase, extracted from Conquest barley harvested during the period 7 to 10 days after anthesis, was purified using acetone fractionation, glycogen complex formation and ion exchange chromatography. The specific activity of the enzyme was increased 750-fold during purification. The purified α-amylase was homogeneous and free of other starch-metabolizing enzymes. Changes in enzyme activity and stability with pH and temperature were studied and the molecular weight and isoelectric point of the enzyme were determined.
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MacGregor et al. (1974) studied this question.
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