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Gliadin proteins in the developing wheat seed
Author(s) -
Mecham Dale K.,
Fullington J. Garrin,
Greene Frank C.
Publication year - 1981
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740320805
Subject(s) - gliadin , chemistry , urea , sodium , gel electrophoresis , polyacrylamide gel electrophoresis , extraction (chemistry) , electrophoresis , ethanol , dry weight , chromatography , botany , biochemistry , biology , gluten , organic chemistry , enzyme
In extracts of developing seeds of wheat ( Triticum aestivum L., cultivars Scout 66, Cheyenne, Nugaines and INIA 66R) examined by polyacrylamide gel electrophoresis, gliadin proteins appeared at 12‐15 days post‐anthesis with mobilities covering nearly the whole range found with mature seeds. Some differences among extractants [2M dimethylformamide (DMF); 2M urea; 60% ethanol; the aluminium lactate‐lactic acid electrophoresis buffer, pH 3.2] in both intensity and occurrence of specific bands were observed. With immature seeds, 60% ethanol extracts produced a maximum number of bands and least background colour, but DMF and urea extracts showed bands from 12‐ to 15‐day seeds at least as well as 60% ethanol extracts despite more background colour. Aluminium lactate buffer extracts occasionally yielded bands not found with other extractants, but gave poor extraction from immature seeds and relatively heavy background staining with mature seeds, especially in the w ‐gliadin (lowest mobility) region. A quantitative sodium dodecyl sulphate‐electrophoresis procedure 1 was used to follow the formation of proteins in various molecular weight ranges (cv. Scout 66 only). At 12‐18 days post‐anthesis, synthesis of protein of molecular weight 30 000‐37 000 accelerated, consistent with the onset and acceleration of formation of α‐, β‐, and some y ‐gliadins. Protein in a band of 44 000 molecular weight formed in similar fashion. In other molecular weight ranges, gliadin bands could not be positively identified because of the complexity of the banding pattern of the total protein.