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Plant Physiology 59:1122-1124 (1977)
© 1977 American Society of Plant Biologists

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Articles

Equal Expression of the Maternal and Paternal Alleles for the Polypeptide Subunits of the Major Storage Protein of the Bean Phaseolus vulgaris L. 1

Timothy C. Hall, Robert C. McLeester and Fredrick A. Bliss

a Department of Horticulture, University of Wisconsin, Madison, Wisconsin 53706

Discontinuous sodium dodecyl sulfate slab gel electrophoresis of G1 globulin from several strains of Phaseolus vulgaris L. seed permitted clear resolution of the constituent polypeptides. Three strains (Tendergreen, Canadian Wonder, and BBL 240) had subunits of molecular weight 53,000, 47,000 and 43,000 while two strains (Seafarer and PI 229,815) had 50,500, 47,000 and 43,000 molecular weight subunits. F1 seed from the cross BBL 240 x PI 229,815 showed four 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 both the maternal and paternal loci for these polypeptides are transcribed and translated with similar efficiency. All of the polypeptides were found to have associated sugar residues.

1 This study was supported by National Science Foundation Grant PCM 74-21675 and by Hatch Projects 1378 and 1626 of the Research Division, College of Agricultural and Life Sciences, University of Wisconsin, Madison.




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A. Zakharov, M. Carchilan, T. Stepurina, V. Rotari, K. Wilson, and I. Vaintraub
A comparative study of the role of the major proteinases of germinated common bean (Phaseolus vulgaris L.) and soybean (Glycine max (L.) Merrill) seeds in the degradation of their storage proteins
J. Exp. Bot., October 1, 2004; 55(406): 2241 - 2249.
[Abstract] [Full Text] [PDF]


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ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1977 by the American Society of Plant Biologists