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Seed Germination Studies. III. Properties of a Cell-Free Amino Acid Incorporating System from Pea Cotyledons; Possible Origin of Cotyledonary α-Amylase

Richard R. Swain and Eugene E. Dekker
Plant Physiology
Vol. 44, No. 3 (Mar., 1969), pp. 319-325
Stable URL: http://www.jstor.org/stable/4261649
Page Count: 7
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Seed Germination Studies. III. Properties of a Cell-Free Amino Acid Incorporating System from Pea Cotyledons; Possible Origin of Cotyledonary α-Amylase
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Abstract

Pea cotyledonary α-amylase increases dramatically both in specific activity and total activity between days 7 to 10 when germination occurs in the dark. This enzymatic activity does not seem to appear as a consequence of release or formation of an activator, removal of an inhibitor, dissociation of an inactive amylase complex, or proteolytic decomposition of a zymogen precursor. The possibility remains that the α-amylase is newly synthesized during germination. The preparation and properties of a cell-free protein-synthesizing system from germinating pea cotyledons is described; polyuridylic acid must be added for L-phenylalanine incorporation. Active microsomal preparations can be obtained from cotyledons germinated 10 days.

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