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

@article{Swain1969SeedGS,
  title={Seed Germination Studies. III. Properties of a Cell-free Amino Acid Incorporating System From Pea Cotyledons; Possible Origin of Cotyledonary $\alpha$-Amylase},
  author={R. Swain and E. E. Dekker},
  journal={Plant Physiology},
  year={1969},
  volume={44},
  pages={319-325}
}
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… Expand

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