Theoretical and Applied Genetics

, Volume 59, Issue 6, pp 349–359 | Cite as

Fractionation of wheat gliadin and glutenin subunits by two-dimensional electrophoresis and the role of group 6 and group 2 chromosomes in gliadin synthesis

  • J. W. S. Brown
  • R. B. Flavell


Subunits of wheat endosperm proteins have been fractionated by two-dimensional electrophoresis. To determine which subunits in the two-dimensional electrophoretic pattern belong to gliadin or glutenin the endosperm proteins have also been fractionated by a modified Osborne procedure and by gel filtration on Sephadex G-100 and Sepharose CL-4B prior to separation by two-dimensional electrophoresis.

The control of production of five major grain protein subunits is shown to be determined by chromosomes 6A, 6B and 6D by comparing two-dimensional electrophoretic protein subunit patterns of aneuploid lines of the variety ‘Chinese Spring’. From these and previous studies it is concluded that some α, β and γ gliadins (molecular weights by SDS-PAGE 30,000 to 40,000) are specified by genes on the short arms of homoeologous Group 6 chromosomes, the ω gliadins (molecular weights by SDS-PAGE 50,000 to 70,000) are specified by genes on the short arms of homoeologous Group 1 chromosomes and the glutenin subunits (molecular weights by SDS-PAGE > 85,000) are specified by genes on the long arms of homoeologous Group 1 chromosomes.

No major gliadins or glutenin subunits were absent when any of the chromosomes in homoeologous Groups 2, 3, 4, 5 or 7 were deleted. However two gliadins whose presumed structural genes are on chromosome 6D were absent in aneuploid stocks of ‘Chinese Spring’ carrying two additional doses of chromosome 2A. Two out of thirty-three intervarietal or interspecific chromosome substitution lines examined, involving homoeologous Group 2 chromosomes, lacked the same two gliadins. All the subunits in the other thirty-one chromosome substitution lines were indistinguishable from those in ‘Chinese Spring’. It is therefore concluded that the major variation affecting gliadin and glutenins in wheat is concentrated on the chromosomes of homoeologous Groups 1 and 6 but Group 2 chromosomes are candidates for further study.

An endosperm protein controlled by chromosome 4D in ‘Chinese Spring’ is shown to be a high molecular weight globulin.


Triticum aestivum Glutenin Gliadin Electrophoresis 


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  1. Beckwith, A.C.; Nielson, H.C.; Wall, J.S.; Huebner, F.R. (1966): Isolation and characterization of a high-molecular weight protein from wheat gliadin. Cereal Chem. 43, 14–29Google Scholar
  2. Bernardin, J.E.; Kasarda, D.D. (1973): The microstructure of wheat protein fibrils. Cereal Chem. 50, 736–745Google Scholar
  3. Bietz, J.A.; Huebner, F.R.; Sanderson, J.E.; Wall, J.S. (1977): Wheat gliadin homology revealed through N-terminal amino acid sequence. Cereal Chem. 54, 1070–1083Google Scholar
  4. Bietz, J.A.; Shepherd, K.W.; Wall, J.S. (1975): Single kernel analysis of glutenin: Use in wheat genetics and breeding. Cereal Chem. 52, 513–532Google Scholar
  5. Bietz, J.A.; Wall, J.S. (1972): Wheat gluten molecules: Molecular weights determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis. Cereal Chem. 49, 416–430Google Scholar
  6. Bietz, J.A.; Wall, J.S. (1973): Isolation and characterization of gliadin-like subunits from glutenin. Cereal Chem. 50, 537–547Google Scholar
  7. Booth, M.R.; Ewart, J.A.D. (1969): Studies on four components of wheat gliadins. Biochim. Biophys. Acta 181, 226–233Google Scholar
  8. Brown, J.W.S.; Kemble, R.J.; Law, C.N.; Flavell, R.B. (1979): Control of endosperm proteins in Triticum aestivum (var. ‘Chinese Spring’) and Aegilops umbellulata by homoeologous group 1 chromosomes. Genetics 93, 189–200Google Scholar
  9. Brown, J.W.S., Law, C.N., Worland, A.J., Flavell, R.B. (1981): Genetic variation in wheat endosperm proteins: an analysis by two dimensional electrophoresis using intervarietal chromosome substitution lines. Theor. Appl. Genet. 59, 361–371Google Scholar
  10. Charbonnier, L. (1973): Etude des protéines alcolo-solubles de la farine de blé. Biochimie 55, 1217–1225Google Scholar
  11. Charbonnier, L. (1974): Isolation and characterization of ω-gliadin fractions. Biochim. Biophys. Acta 359, 142–151Google Scholar
  12. Chen, C.H.; Bushuk, W. (1970): Nature of proteins in Triticale and its parental species. I. Solubility characteristics and amino acid composition of endosperm proteins. Canad. J. Plant Sci. 50, 9–14Google Scholar
  13. Hamauzu, Z.; Kamazuka, Y.; Kanazawa, H.; Yonezawa, D. (1975): Molecular weight determination of component polypeptides of glutenin after fractionation by gel filtration. Agr. Biol. Chem. 39, 1527–1531Google Scholar
  14. Hamauzu, Z.; Toyomasu, T.; Tonezawa, D. (1974): Molecular weight determination of gliadin fractions in gel filtration by SDS-Polyacrylamide gel electrophoresis and sedimentation equilibrium. Agr. Biol. Chem. 38, 2445–2450Google Scholar
  15. Huebner, F.R.; Wall, J.S. (1976): Fractionation and quantitative differences of glutenin from wheat varieties varying in baking quality. Cereal Chem. 53, 258–268Google Scholar
  16. Jones, R.W.; Taylor, N.W.; Senti, F.R. (1959): Electrophoresis and fractionation of wheat gluten. Arch. Biochem. Biophys. 84, 363–376Google Scholar
  17. Law, C.N.; Young, C.F.; Brown J.W.S.; Snape, J.W.; Worland, A.J. (1978): The study of grain protein control in wheat using whole chromosome substitution lines. In: Seed protein Improvement by Nuclear Techniques, pp. 483–502. Vienna: Intern. Atomic Energy AgencyGoogle Scholar
  18. Nielson, H.C.; Babcock, G.E.; Senti, F.R. (1962): Molecular weight studies on glutenin before and after disulphide-bond splitting. Arch. Biochem. Biophys. 96, 252–258Google Scholar
  19. O'Farrell, P.H. (1975): High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007–4021Google Scholar
  20. Osborne, T.B. (1907): Proteins of the Wheat Kernel. Washington D.C.: Carnegie Institute of WashingtonGoogle Scholar
  21. Payne, P.I.; Corfield, K.G. (1979): Subunit of wheat glutenin proteins isolated by gel filtration in a dissociating medium. Planta 145, 83–88Google Scholar
  22. Riley, R.; Chapman, V.; Johnson, R. (1968): Introduction of yellow rust resistance of Aegilops comosa into wheat by genetically induced homoeologous recombinations. Nature 217, 383–384Google Scholar
  23. Sears, E.R. (1954): The aneuploids of common wheat. Res. Bull. Mo. Coll. Agr. Exp. Sta. 572, 58Google Scholar
  24. Sexson, K.; Wu, Y.V.; Huebner, F.R.; Wall, J.S. (1978): Molecular weights of wheat γ 2, β 6, α 1, α 8 and α 9 gliadins. Biochim. Biophys. Acta. 532, 279–285Google Scholar
  25. Shepherd, K.W. (1968): Chromosomal control of endosperm proteins in wheat and rye. In: 3rd Int. Wheat Genet. Symp. (eds.: Finlay, K.W.; Shepherd, K.W.), pp. 86–96. New York: Plenum Publ.Google Scholar
  26. Shepherd, K.W. (1973): Homoeology of wheat and alien chromosomes controlling endosperm protein phenotypes. In: Proc. 4th Int. Wheat Genet. Symp. (eds.: Sears, E.R.; Sears, L.M.) pp. 745–760. Columbia Mo.: Agr. Exp. Sta. Univ. Mo.Google Scholar
  27. Waines, J.G. (1973): Chromosomal location of genes controlling endosperm protein production in Triticum aestivum cv. ‘Chinese Spring’. In: Proc. 4th Int. Wheat Genet. Symp. (eds.: Sears, E.R.; Sears, L.M.S.), pp. 873–877. Columbia Mo.: Agr. Exp. Stn. Univ. Mo.Google Scholar
  28. Woychik, J.H.; Boundy, J.A.; Dimler, R.J. (1961): Starch gel electrophoresis of wheat gluten proteins with concentrated urea. Arch. Biochem. Biophys. 94, 477–482Google Scholar
  29. Woychik, J.H.; Huebner, F.R.; Dimler, R.J. (1964): Reduction and starch gel electrophoresis of wheat gliadin and glutenin. Arch. Biochem. Biophys. 105, 151–156Google Scholar
  30. Wrigley, C.W.; Shepherd, K.W. (1973): Electrofocusing of grain proteins from wheat genotypes. Ann. N.Y. Acad. Sci. 209, 154–162Google Scholar

Copyright information

© Springer-Verlag 1981

Authors and Affiliations

  • J. W. S. Brown
    • 1
    • 2
  • R. B. Flavell
    • 1
  1. 1.Plant Breeding InstituteCambridgeEngland
  2. 2.Agrigenetics Research ParkMadisonUSA

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