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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
Author(s) -
Ranjita Swain,
Eugene E. Dekker
Publication year - 1969
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.44.3.319
Subject(s) - germination , amylase , cotyledon , botany , biology , amino acid , biochemistry , chemistry , enzyme
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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