Abstract
The accumulation of salt-soluble proteins in the endosperm of developing barley (Hordeum vulgare L.) grains was examined. Detached spikes of barley were cultured at different levels of nitrogen nutrition and pulse-labeled with [14C] sucrose at specific times after anthesis. Proteins were extracted from isolated endosperms and separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and crossed immunoelectrophoresis. Fluorography revealed an early, middle and late synthesis of specific proteins during grain filling. Synthesis of proteins appearing at the later stages responded to increased nitrogen nutrition. Two major components, β-amylase and protein Z in particular, had a synthesis profile almost identical to that of the endosperm storage protein, hordein.
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Abbreviations
- CIE:
-
Crossed immunoelectrophoresis
- SDSPAGE:
-
Sodium dodecyl sulphate polyacrylamide gel electrophoresis
References
Chamberlain, J.P. (1979) Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate. Anal. Biochem. 98, 132–135
Doll, H. (1983) Barley seed proteins and possibilities for their improvement. In: Seed proteins. Biochemistry, genetics, nutritive value, pp. 207–224, Gottschalk, W., Müller, H.P., eds. Nijhoff/Dr. Junk, The Hague
Doll, H., Andersen, B. (1981) Preparation of barley storage protein, hordein, for analytical sodium dodecyl sulphatepolyacrylamide gel electrophoresis. Anal. Biochem. 115, 61–66
Giese, H., Andersen, B., Doll, H. (1983) Synthesis of the major storage protein, hordein, in barley. Pulse labeling study of grain filling in liquid cultured detached spikes. Planta 159, 60–65
Hejgaard, J. (1976) Free and protein-bound β-amylases of barley grain. Characterization by two-dimensional immunoelectrophoresis. Physiol. Plant. 38, 293–299
Hejgaard, J. (1982) Purification and properties of protein Z — a major albumin of barley endosperm. Physiol. Plant. 54, 174–182
Hejgaard, J., Bøg-Hansen, T.C. (1974) Quantitative immunoelectrophoresis of barley and malt proteins. J. Inst. Brew. London 80, 436–442
Hejgaard, J., Boisen, S. (1980) High-lysine proteins in Hiproly barley breeding: identification, nutritional significance and new screening methods. Hereditas 93, 311–320
Kirkman, M.A., Shewry, P.R., Miflin, B.J., (1982) The effect of nitrogen nutrition on the lysine content and protein composition of barley seeds. J. Sci. Food Agric. 33, 115–127
Kirsi, M. (1973) Formation of proteinase inhibitors in developing barley grain. Physiol. Plant. 29, 141–144
Kreis, M., Doll, H. (1980) Starch and prolamin level in single and double high-lysine barley mutants. Physiol. Plant. 48, 139–143
Laskey, R.A., Mills, A.D. (1975) Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur. J. Biochem. 56, 335–341
Nelson, O.E. (1969) Genetic modification of protein quality in plants. Adv. Agron. 21, 171–194
Nielsen, G., Johansen, H., Jensen, J., Hejgaard, J. (1983) Localization on barley chromosome 4 of genes coding for β-amylase (Bmy 1) and protein Z (Paz 1). Barley Genet. Newslett. 13, 55–57
Rahman, S., Shewry, P.R., Miflin, B.J. (1982) Differential protein accumultion during barley grain development. J. Exp. Bot. 33, 717–728
Shewry, P.R., Faulks, A.J., Pickerling, R.A., Jones, I.T., Finch, R.A., Miflin, B.J. (1980) The genetic analysis of barley storage proteins. Hereditas 44, 383–389
Visuri, K., Nummi, M. (1972) Purification and characterization of crystalline β-amylase from barley. Eur. J. Biochem. 28, 555–565
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Giese, H., Hejgaard, J. Synthesis of salt-soluble proteins in barley. Pulse-labeling study of grain filling in liquid-cultured detached spikes. Planta 161, 172–177 (1984). https://doi.org/10.1007/BF00395478
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DOI: https://doi.org/10.1007/BF00395478