Electrophoresis of the Soluble Proteins of Wheat Leaf

Abstract

THERE have been several reports of gel electrophoretic separations of leaf proteins. Four components were reported for cabbage leaf¹, seven bands for rice leaf², and about six bands for bean leaf³. Bean leaf proteins have also been studied by Racusen and Calvanico⁴ using preparative gel electrophoresis. Steward and Barber³ obtained good electrophoretic fractionation of the soluble proteins of Neurospora crassa, but observed that extracts from tissues of higher plants yielded bands which were less discrete against a diffuse background. The present paper describes the electrophoresis of the soluble proteins of wheat leaf on 7.5 per cent polyacrylamide gel using a discontinuous tris chloride–tris glycinate buffer system. The method used gave a well-defined pattern and separated more components than reported previously for leaf tissues.