The interaction of proteins during gel electrophoresis

Abstract

Reversible polymerisation and A + B ⇌ C type reactions among proteins during zone electrophoresis may give rise to tailing, extra bands and mobility changes. One or more of these signs are likely to appear with the milder type of interaction, i.e. equilibrium constant in the range 102–108, whether the time to equilibrium is measured in hours or less. Two‐dimensional electrophoresis is more useful for diagnosing interactions. No definite evidence has been obtained for protein‐protein interactions among the slow‐moving gliadins of Bison and Cappelle varieties and the total number of bands probably represents the minimum number of molecular species present. The electrophoretic pattern of a given variety does not appear to alter qualitatively when the year or place of growth is changed. It is estimated that a wheat protein concentration needs to be above ∼0·1 mg/ml to be observable on a starch gel.

Structural studies on wheat (Triticum aestivum) proteins lacking phenylalanine and histidine residues

“…Starch-gel electrophoresis was performed at pH3.2 in aluminium lactate buffer (Ewart, 1966). CNBr peptides were run for 3.5h at IOV/cm.…”

The effect of individual rye chromosomes on the amino acid content of wheat grains

“…This was carried out with 0-008 M aluminium lactate buffer at pH 3-3 as described previously (Ewart, 1966) except that water cooling was used. The 'Perspex' trough was modified so that tap water could be circulated below the gel platform and also through a 'Melinex '-insulated copper vessel lying on top of the gel.…”