The purification and characterization of homologous high molecular weight storage proteins from grain of wheat, rye and barley

Author:

Field J. M.,Shewry P. R.,Miflin B. J.,March J. F.

Publisher

Springer Science and Business Media LLC

Subject

Genetics,Agronomy and Crop Science,General Medicine,Biotechnology

Reference61 articles.

1. Bernardin, J.E. (1978): Gluenin protein interaction with small molecules and ions — the control of flour properties. Bakers Digest 52, 20–23

2. Bietz, J.A.; Huebner, F.R.; Sandersen, J.E.; Wall, J.S. (1977): Wheat gliadin homology revealed through N-terminal amino acid sequence analysis. Cereal Chem. 54, 1070–1083

3. Bietz, J.A.; Shepherd, K.W.; Wall, J.S. (1975): Single kernal analysis of glutenin: use in wheat genetics and breeding. Cereal Chem. 52, 513–532

4. Bietz, J.A.; Wall, J.S. (1972): Wheat gluten subunits: molecular weights determined by sodium dodecylsulphate polyacrylamide gel electrophoresis. Cereal Chem. 49, 416–430

5. Bietz, J.A.; Wall, J.S. (1973): Isolation and characterization of gladin-like subunits from glutenin. Cereal Chem. 50, 537–547

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