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. 1969 Mar;44(3):319–325. doi: 10.1104/pp.44.3.319

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

Richard R Swain a,2, Eugene E Dekker a
PMCID: PMC396085  PMID: 5775202

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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