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Plant Physiology 44:319-325 (1969)
© 1969 American Society of Plant Biologists

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Articles

Seed Germination Studies. III. Properties of a Cell-free Amino Acid Incorporating System From Pea Cotyledons; Possible Origin of Cotyledonary {alpha}-Amylase 1

Richard R. Swain2 and Eugene E. Dekker

a Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48104

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.


2 National Science Foundation Fellow (1963-64) and a Graduate School Predoctoral Fellow, The University of Michigan (1964-65). Present address: Department of Biology, MacMurray College, Jacksonville, Illinois 62650.

1 Supported by Grant AM-03718 from the National Institute of Arthritis and Metabolic Diseases, United States Public Health Service.







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ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1969 by the American Society of Plant Biologists