Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1973 Aug;52(2):98–104. doi: 10.1104/pp.52.2.98

Isolation and Characterization of Glucosamine-containing Storage Glycoproteins from the Cotyledons of Phaseolus aureus1

Mary C Ericson a, Maarten J Chrispeels a,2
PMCID: PMC366448  PMID: 16658529

Abstract

Cotyledons of Phaseolus aureus contain protein-bound glucosamine which is metabolized during germination. The glucosamine is present in storage glycoproteins, and these are concurrently metabolized along with the glucosamine. These glycoproteins are associated with protein bodies. Characterization of the glucosamine-containing storage proteins showed them to be identical with vicilin and legumin, the major storage proteins of the Leguminosae. Phaseolus aureus vicilin has a sedimentation constant of 8.0S and is made up of four nonidentical subunits. It contains 0.2% glucosamine and 1% mannose. Legumin has a sedimentation constant of 11.3S and is made up of three nonidentical subunits. It contains about 0.1% glucosamine.

Full text

PDF
98

Images in this article

102Image
on p.102
103Image
on p.103

Selected References

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

  1. BOAS N. F. Method for the determination of hexosamines in tissues. J Biol Chem. 1953 Oct;204(2):553–563. [PubMed] [Google Scholar]
  2. Bailey C. J., Boulter D. The structure of legumin, a storage protein of broad bean (Vicia faba) seed. Eur J Biochem. 1970 Dec;17(3):460–466. doi: 10.1111/j.1432-1033.1970.tb01187.x. [DOI] [PubMed] [Google Scholar]
  3. Chin T. Y., Poulson R., Beevers L. The Influence of Axis Removal on Protein Metabolism in Cotyledons of Pisum sativum L. Plant Physiol. 1972 Apr;49(4):482–489. doi: 10.1104/pp.49.4.482. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  5. Danielsson C. E. Seed globulins of the Gramineae and Leguminosae. Biochem J. 1949;44(4):387–400. doi: 10.1042/bj0440387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. GRANT D. R., LAWRENCE J. M. EFFECTS OF SODIUM DODECYL SULFATE AND OTHER DISSOCIATING REAGENTS ON THE GLOBULINS OF PEAS. Arch Biochem Biophys. 1964 Dec;108:552–561. doi: 10.1016/0003-9861(64)90441-2. [DOI] [PubMed] [Google Scholar]
  7. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  8. MARTIN R. G., AMES B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J Biol Chem. 1961 May;236:1372–1379. [PubMed] [Google Scholar]
  9. Millerd A., Simon M., Stern H. Legumin Synthesis in Developing Cotyledons of Vicia faba L. Plant Physiol. 1971 Oct;48(4):419–425. doi: 10.1104/pp.48.4.419. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. PUSZTAI A. HEXOSAMINES IN THE SEEDS OF HIGHER PLANTS (SPERMATOPHYTES). Nature. 1964 Mar 28;201:1328–1329. doi: 10.1038/2011328b0. [DOI] [PubMed] [Google Scholar]
  11. Roberts R. M., Cetorelli J. J., Kirby E. G., Ericson M. Location of glycoproteins that contain glucosamine in plant tissues. Plant Physiol. 1972 Nov;50(5):531–535. doi: 10.1104/pp.50.5.531. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Roberts R. M. The incorporation of D-glucosamine-14C into root tissues of higher plants. Plant Physiol. 1970 Mar;45(3):263–267. doi: 10.1104/pp.45.3.263. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Varner J. E., Balce L. V., Huang R. C. Senescence of Cotyledons of Germinating Peas. Influence of Axis Tissue. Plant Physiol. 1963 Jan;38(1):89–92. doi: 10.1104/pp.38.1.89. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Varner J. E., Schidlovsky G. Intracellular Distribution of Proteins in Pea Cotyledons. Plant Physiol. 1963 Mar;38(2):139–144. doi: 10.1104/pp.38.2.139. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES