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. 1985 May;78(1):172–177. doi: 10.1104/pp.78.1.172

Biochemical Characterization of Rice Glutelin 1

Tuan-Nan Wen 1, Dawn S Luthe 1
PMCID: PMC1064697  PMID: 16664193

Abstract

The two major subunits of rice glutelin, the acidic (α) and basic (β) polypeptides were purified by chromatofocusing and cation exchange chromatography, respectively. The molecular weight range of the α polypeptides was 28.5 to 30.8 kilodaltons and the molecular weight range of the β polypeptides was 20.6 to 21.6 kilodaltons. Electrofocusing in polyacrylamide gels showed that the isoelectric points of the α and β polypeptides were 6.5 to 7.5 and 9.4 to 10.3, respectively. At least 12 polypeptides of the α-group and nine polypeptides of the β-group could be separated by electrofocusing. The amino acid compositions of whole glutelin, and the purified α and β subunits were analyzed. The α subunit contained more glutamic acid/glutamine, serine, and glycine, and less alanine, lysine, aspartic acid/asparagine, and isoleucine than the β subunit. A comparison of the amino acid composition of rice glutelin subunits with those of the 11S proteins from eight other plant species indicated that there is more similarity between the β subunits than the α subunits of several diverse plant species.

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Selected References

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

  1. Adeli K., Altosaar I. Role of endoplasmic reticulum in biosynthesis of oat globulin precursors. Plant Physiol. 1983 Dec;73(4):949–955. doi: 10.1104/pp.73.4.949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Barton K. A., Thompson J. F., Madison J. T., Rosenthal R., Jarvis N. P., Beachy R. N. The biosynthesis and processing of high molecular weight precursors of soybean glycinin subunits. J Biol Chem. 1982 Jun 10;257(11):6089–6095. [PubMed] [Google Scholar]
  3. Brinegar A. C., Peterson D. M. Separation and characterization of oat globulin polypeptides. Arch Biochem Biophys. 1982 Nov;219(1):71–79. doi: 10.1016/0003-9861(82)90135-7. [DOI] [PubMed] [Google Scholar]
  4. Brinegar A. C., Peterson D. M. Synthesis of Oat Globulin Precursors : Analogy to Legume 11S Storage Protein Synthesisa. Plant Physiol. 1982 Dec;70(6):1767–1769. doi: 10.1104/pp.70.6.1767. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cornish-Bowden A. Critical values for testing the significance of amino acid composition indexes. Anal Biochem. 1980 Jul 1;105(2):233–238. doi: 10.1016/0003-2697(80)90450-9. [DOI] [PubMed] [Google Scholar]
  6. Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry. 1967 Jul;6(7):1948–1954. doi: 10.1021/bi00859a010. [DOI] [PubMed] [Google Scholar]
  7. Ereken-Tumer N., Richter J. D., Nielsen N. C. Structural characterization of the glycinin precursors. J Biol Chem. 1982 Apr 25;257(8):4016–4018. [PubMed] [Google Scholar]
  8. Inglis A. S., Liu T. Y. The stability of cysteine and cystine during acid hydrolysis of proteins and peptides. J Biol Chem. 1970 Jan 10;245(1):112–116. [PubMed] [Google Scholar]
  9. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  10. Moreira M. A., Hermodson M. A., Larkins B. A., Nielsen N. C. Comparison of the primary structure of the acidic polypeptides of glycinin. Arch Biochem Biophys. 1981 Sep;210(2):633–642. doi: 10.1016/0003-9861(81)90230-7. [DOI] [PubMed] [Google Scholar]
  11. Moreira M. A., Hermodson M. A., Larkins B. A., Nielsen N. C. Partial characterization of the acidic and basic polypeptides of glycinin. J Biol Chem. 1979 Oct 10;254(19):9921–9926. [PubMed] [Google Scholar]
  12. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  13. O'Farrell P. Z., Goodman H. M., O'Farrell P. H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell. 1977 Dec;12(4):1133–1141. doi: 10.1016/0092-8674(77)90176-3. [DOI] [PubMed] [Google Scholar]
  14. Peterson D. M. Subunit structure and composition of oat seed globulin. Plant Physiol. 1978 Oct;62(4):506–509. doi: 10.1104/pp.62.4.506. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Rossi H. A., Luthe D. S. Isolation and characterization of oat globulin messenger RNA. Plant Physiol. 1983 Jun;72(2):578–582. doi: 10.1104/pp.72.2.578. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Staswick P. E., Hermodson M. A., Nielsen N. C. Identification of the acidic and basic subunit complexes of glycinin. J Biol Chem. 1981 Aug 25;256(16):8752–8755. [PubMed] [Google Scholar]
  17. Walburg G., Larkins B. A. Oat seed globulin: subunit characterization and demonstration of its synthesis as a precursor. Plant Physiol. 1983 May;72(1):161–165. doi: 10.1104/pp.72.1.161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Wallace R. W., Dieckert J. W. Isolation of coconut storage proteins by polyacrylamide-gel electrophoresis. Anal Biochem. 1976 Oct;75(2):498–508. doi: 10.1016/0003-2697(76)90105-6. [DOI] [PubMed] [Google Scholar]
  19. Wright D. J., Boulter D. Purification and subunit structure of legumin of Vicia faba L. (broad bean). Biochem J. 1974 Aug;141(2):413–418. doi: 10.1042/bj1410413. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Yamagata H., Sugimoto T., Tanaka K., Kasai Z. Biosynthesis of storage proteins in developing rice seeds. Plant Physiol. 1982 Oct;70(4):1094–1100. doi: 10.1104/pp.70.4.1094. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Zacharius R. M., Zell T. E., Morrison J. H., Woodlock J. J. Glycoprotein staining following electrophoresis on acrylamide gels. Anal Biochem. 1969 Jul;30(1):148–152. doi: 10.1016/0003-2697(69)90383-2. [DOI] [PubMed] [Google Scholar]

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