Electrophoretic analysis of flour proteins I.—‚salt‐soluble’︁ proteins

Abstract

AbstractExtracts of a soft wheat patent flour have been examined with moving‐boundary electrophoresis. The six buffers investigated produced different distribution patterns, all with satisfactory enantiography. Veronal buffer, pH 8.6, T/2 0.1, was the most useful, showing at least nine components when 0.1M‐sodium chloride was the extractant, while phosphate buffer, pH 3.2, T/2 0.05, was the least satisfactory, yielding only three general electrophoretic regions. Flour was extracted with solutions of varying pH and ionic strength and the extracts electrophoretically analysed in veronal buffer. Nearly all the components observed in the 0.1M‐sodium chloride extract were present, at least to some extent, in all the other extracts. Extraction and electrophoretic analysis in acetate buffer disclosed differences in component distribution when compared with the 0.1M‐sodium chloride extract. No significant differences were observed in a similar study with borate buffer. An extract of a defatted flour differed slightly in its distribution pattern from an extract of an intact flour.