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. 1971 Jan;47(1):119–123. doi: 10.1104/pp.47.1.119

The Fate of l-Phenylalanine Fed to Germinating Pea Seeds, Pisum sativum (L.) var. Alaska, during Imbibition 1

Constance Nozzolillo a, K B Paul a,2, C Godin a,3
PMCID: PMC365823  PMID: 16657566

Abstract

Radioactive l-phenylalanine-l-14C or -U-14C was fed to pea seeds during imbibition. More than 95% was imbibed. Less than 1% of the radioactivity was respired as CO2. Of the radioactivity taken into the embryos, 80% was still in the cotyledons by 3 days. About half of this was unchanged phenylalanine: 5% free, 10 to 20% in soluble proteins, 1 to 6% in cell wall proteins, and 14% released by mild acid hydrolysis. No other radioactive amino acid was found. About 0.3% of the radioactivity was identified as free caffeic, ferulic, and coumaric acids or their glycosides, and a further 5% was released by mild acid hydrolysis into a phenolic acid fraction. About half of the radioactivity in the cotyledons was lost in the fractionation procedures.

About 20% of the radioactivity was found in the shootroot axes to which it had been translocated. Phenylalanine accounted for nearly all the identifiable radioactivity: about 1% free, 1 to 3% in soluble proteins, 1 to 5% in cell wall proteins, and 1% bound to insoluble fractions from which it was released by mild acid hydrolysis. About 1% was released into a phenolic acid fraction. About half of the radioactivity in the shoot-root axes was lost in the fractionation procedures.

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Selected References

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

  1. Bishop C. T., Bayley S. T., Setterfield G. Chemical Constitution of the Primary Cell Walls of Avena Coleoptiles. Plant Physiol. 1958 Jul;33(4):283–289. doi: 10.1104/pp.33.4.283. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. KOUKOL J., CONN E. E. The metabolism of aromatic compounds in higher plants. IV. Purification and properties of the phenylalanine deaminase of Hordeum vulgare. J Biol Chem. 1961 Oct;236:2692–2698. [PubMed] [Google Scholar]
  3. Larson L. A., Beevers H. Amino Acid Metabolism in Young Pea Seedlings. Plant Physiol. 1965 May;40(3):424–432. doi: 10.1104/pp.40.3.424. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Lawrence J. M., Grant D. R. Nitrogen Mobilization in Pea Seedlings. II. Free Amino Acids. Plant Physiol. 1963 Sep;38(5):561–566. doi: 10.1104/pp.38.5.561. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Partridge S. M. Displacement chromatography on synthetic ion-exchange resins. 3. Fractionation of a protein hydrolysate. Biochem J. 1949;44(5):521–527. [PMC free article] [PubMed] [Google Scholar]
  6. Rosa N., Neish A. C. Formation and occurrence of N-malonylphenylalanine and related compounds in plants. Can J Biochem. 1968 Aug;46(8):799–806. [PubMed] [Google Scholar]
  7. WATKIN J. E., UNDERHILL E. W., NEISH A. C. Biosynthesis of quercetin in buckwheat. II. Can J Biochem Physiol. 1957 Mar;35(3):229–237. [PubMed] [Google Scholar]
  8. YOUNG J. L., VARNER J. E. Enzyme synthesis in the cotyledons of germinating seeds. Arch Biochem Biophys. 1959 Sep;84:71–78. doi: 10.1016/0003-9861(59)90555-7. [DOI] [PubMed] [Google Scholar]

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