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  • Title: Seed germination studies. 3. Properties of a cell-free amino acid incorporating system from pea cotyledons; possible origin of cotyledonary alpha-amylase.
    Author: Swain RR, Dekker EE.
    Journal: Plant Physiol; 1969 Mar; 44(3):319-25. PubMed ID: 5775202.
    Abstract:
    Pea cotyledonary alpha-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 alpha-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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