Abstract
An antiserum to subunit 2 from the high-molecular-weight (HMW) subunits of the glutenin fraction of Triticum aestivum cv. Highbury was shown to react with related subunits from other cultivars of wheat. The reaction was measured quantitatively by laser nephelometry in polyethylene glycol phosphate-buffered saline after dissolving the HMW fraction in 0.1 M acetic acid; urea used to dissolve the HMW prolamins inhibited the reaction, in some cases at the low concentration of 0.06 M. A study of the comparative reactions of other cereal prolamins was made. ‘D’ hordein, the homologous HMW protein of barley, showed less reaction, which was more inhibited by urea than the wheat subunits. Some ω-gliadins from the wheat cultivars Chinese Spring and Cheyenne reacted more strongly than the injected fraction and there was less inhibition by urea. A-, β- and γ3 of wheat also reacted with the antiserum while a secalin of rye of Mr 40000 gave a weak reaction.
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Abbreviations
- HMW:
-
high molecular weight
- PAGE:
-
polyacrylamide-gel electrophoresis
- PBS:
-
phosphate-buffered saline
- PE:
-
pyridylethylated
- SDS:
-
sodium dodecyl sulphate
References
Bietz, J.A., Wall, J.S. (1980) Identity of high molecular weight gliadin and ethanol-soluble glutelin subunits of wheat: relation to gluten structure. Cereal Chem. 57, 415–421
Bright, S.W.J., Shewry, P.R. (1983) Improvement of protein quality in cereals. CRC Crit. Rev. Plant Sci. 1, 49–93
Charbonnier, L., Jos, J., Mougenot, J.F., Mossé, J. (1980) Toxicité comparée de différentes céréales pour les sujets intolérants au gluten. Reprod. Nutr. Dév. 20, 1369–1377
Ewart, J.A.D. (1977) Immunochemistry of wheat proteins. In: Immunological aspects of foods, pp. 87–116, Catsimpoolas, N., ed. The Avi Publishing Company Inc., Westport, Connecticut
Festenstein, G.N., Hay, F.C. (1982) Immunochemical studies on barley seed storage proteins. Plant Sci. Lett. 26, 199–209
Festenstein, G.N., Hay, F.C., Miflin, B.J., Shewry, P.R. (1984) Immunochemical studies on barley seed storage proteins. The specificity of an antibody to ‘C’ hordein and its reaction with prolamins from other cereals. Planta 162, 524–531
Field, J.M., Shewry, P.R., Miflin, B.J., March, J.F. (1982) The purification and characterization of homologous high molecular weight storage proteins from grain of wheat, rye and barley. Theor. Appl. Genet. 62, 329–336
Field, J.M., Shewry, P.R., Miflin, B.J. (1983) Aggregation states of alcohol-soluble storage proteins of barley, rye, wheat and maize, J. Sci. Food Agric. 34, 362–369
Forde, J., Forde, B.G., Fry, R.P., Kreis, M., Shewry, P.R., Miflin, B.J. (1983) Identification of barley and wheat cDNA clones related to the high-Mr polypeptides of wheat gluten. FEBS Lett. 162, 360–366
Friedman, M., Krull, L.H., Cavins, J.F. (1970) The chromatographic determination of cystine and cysteine residues in proteins as S-β-(4-pyridylethyl)cysteine. J. Biol. Chem. 245, 3868–3871
Hopp, T.P., Woods, K.R. (1981) Prediction of protein antigenic determinants from amino acid sequences. Proc. Natl. Acad. Sci. USA 78, 3824–3828
Kasarda, D.D. (1978) The relationship of wheat proteins to coeliac disease. Cereals Foods World 23, 240–244
Kasarda, D.D., Autran, J-C., Lew, E.J.-L., Nimmo, C.C., Shewry, P.R. (1983) N-terminal amino acid-sequences of ω-gliadins and ω-secalins: implications for the evolution of prolamin genes. Biochim. Biophys. Acta 747, 138–150
Khan, K., Bushuk, W. (1979) Studies of glutenin. XIII. Gel filtration, isoelectric focusing, and amino acid composition studies. Cereal Chem. 56, 505–512
Kieffer M., Frazier, P.J., Daniels, N.W.R., Coombs, R.R.A. (1982) Wheat gliadin fractions and other cereal antigens reactive with antibodies in the sera of coeliac patients. Clin. Exp. Immunol. 50, 651–660
Kreis, M., Shewry, P.R., Forde, B.G., Rahman, S., Bahramian, M.B., Miflin, B.J. (1984) Molecular analysis of the effects of the mutant lys3a gene on the expression of Hor loci in developing endosperms of barley (Hordeum vulgare L.). Biochem. Genet. 22, 231–255
Mäkelä, O. (1965) Single lymph node cells producing heteroclitic bacteriophage antibody. J. Immunol. 95, 378–386
Payne, P.I., Law, C.N., Mudd, E.E. (1980) Control by homocologous group 1 chromosomes of the high-molecular-weight subunits of glutenin, a major protein of wheat endosperm. Theor. Appl. Genet. 58, 113–120
Payne, P.I., Corfield, K.G., Holt, L.M., Blackman, J.A. (1981a) Correlations between the inheritance of certain high-molecular-weight subunits of glutenin and bread-making quality in progenies of six crosses of bread wheat. J. Sci. Food Agric. 32, 51–60
Payne, P.I., Holt, L.M., Law, C.N. (1981b) Structural and genctical studies on the high-molecular-weight subunits of wheat glutenin. I. Allelic variation in subunits amongst varieties of wheat (Triticum aestivum). Theor. Appl.Genet. 60, 229–236
Payne, P.I., Holt, L.M., Worland, A.J., Law, C.N. (1982) Structural and genetical studies on the high-molecular-weight subunits of wheat glutenin. III. Telocentric mapping of the subunit genes on the long arms of the homoeologous group 1 chromosomes. Theor. Appl. Genet. 63, 129–138
Shewry, P.R., Hill, J.M., Pratt, H.M., Leggatt, M.M., Miflin, B.J. (1978) An evaluation of techniques for the extraction of hordein and glutelin from barley seed and a comparison of the protein composition of Bomi and Risø 1508. J. Exp. Bot. 29, 677–692
Shewry, P.R., Field, J.M., Kirkman, M.A., Faulks, A.J., Miflin, B.J. (1980) The extraction, solubility and characterization of two groups of barley storage polypeptides. J. Exp. Bot. 31, 393–407
Shewry, P.R., Field, J.M., Lew, E.J.-L., Kasarda, D.D. (1982) The purification and characterization of two groups of storage proteins (secalins) from rye (Secale cereale L.) J. Exp. Bot. 33, 261–268
Shewry, P.R., Miflin, B.J., Lew, E.J.-L., Kasarda, D.D. (1983) The preparation and characterization of an aggregated gliadin fraction from wheat. J. Exp. Bot. 34, 1403–1410
Shewry, P.R., Field, J.M., Faulks, A.J., Parmar, S., Miflin, B.J., Dietler, M.D., Lew, E.J.-L., Kasarda, D.D. (1984a) The purification and N-terminal amino acid sequence analysis of the high molecular weight gluten polypeptides of wheat. Biochim. Biophys. Acta 788, 23–34
Shewry, P.R., Miflin, B.J., Kasarda, D.D. (1984b) The structural and evolutionary relationships of the prolamin storage proteins of barley, rye and wheat. Philos. Trans. R. Soc. London Ser. B 304, 297–308
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Festenstein, G.N., Hay, F.C., Miflin, B.J. et al. Specificity of an antibody to a subunit of high-molecular-weight storage protein from wheat seed and its reaction with other cereal storage proteins (prolamins). Planta 164, 135–141 (1985). https://doi.org/10.1007/BF00391039
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DOI: https://doi.org/10.1007/BF00391039