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Elektrochemisches Verhalten harnstofflöslicher Komponenten von Weizenkleberproteinen
Author(s) -
Günzel G.
Publication year - 1976
Publication title -
zeitschrift für pflanzenernährung und bodenkunde
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.644
H-Index - 87
eISSN - 1522-2624
pISSN - 0044-3263
DOI - 10.1002/jpln.19761390205
Subject(s) - chromatography , chemistry , isoelectric point , urea , isoelectric focusing , gluten , electrophoresis , polyacrylamide gel electrophoresis , glutenin , biochemistry , enzyme , protein subunit , gene
Electrochemical Behavior of Urea Soluble Components of Gluten Proteins of Wheat Protein zones of urea soluble gluten proteins of wheat samples from different cultivars and locations were analyzed after 2 dimensional separation by sucrose‐density‐gradient isoelectric focusing and disk polyacrylamide‐gel electrophoresis. More than 50% of the urea soluble proteins was focused in a range from pH 6,5–7,6. The major concentration in all samples was observed close to pH 7,0 as indicated by the main peak in all absorption diagrams. Electrophoretic separation of proteins of equal isoelectric characteristics yielded fractions differing mainly in charges. Two dimensional separation yielded more than 40 protein fractions. The pattern of these fractions was more influenced by environmental effects than by cultivars. No relation between protein pattern and baking quality was observed.