Equal Expression of the Maternal and Paternal Alleles for the Polypeptide Subunits of the Major Storage Protein of the Bean Phaseolus vulgaris L.

Abstract

Discontinuous sodium dodecyl sulfate slab gel electrophoresis of G1 globulin from several strains of P. vulgaris L. seed permitted clear resolution of constituent polypeptides. Three strains (Tendergreen, Canadian Wonder and BBL 240) had subunits of MW 53,000, 47,000 and 43,000 while 2 strains (Seafarer and PI 229,815) had 50,500, 47,000 and 43,000 MW . F1 seed from the cross BBL 240 .times. PI 229,815 showed 4 polypeptides on dissociation of the G1 protein; however, the amount of each of the 53,000 and 50,500 subunits was half that of the 47,000 subunit. This is interpreted as evidence that the maternal and paternal loci for these polypeptides are transcribed and translated with similar efficiency. All of the polypeptides apparently have associated sugar residues.