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The structure and complexity of the 11S polypeptides in soybeans

  • Technical
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Journal of the American Oil Chemists’ Society

Abstract

The 11S soybean proteins called glycinin are isolated as a 350,000 dalton complex that consists of six nonidentical subunits. Each subunit consists of an acidic polypeptide component linked to a basic component by a single disulfide bond. Initial translation products of glycinin subunits are single polypeptides of ca. 60,000 daltons that undergo both co- and posttranslational modification. The precursors have a short signal sequence, followed by the acidic component, a short linker polypeptide, the basic component and a short trailer peptide. Five major subunit types have been purified and characterized by amino acid sequence analysis. While all of them are clearly synthesized by a family of homologous genes, they can be separated into two groups based on sequence homologies. Group I subunits (A1aB2, A1bB1b, A12B1a) are uniform in size (Mr = 58,000), relatively rich in methionine, and exhibit ca. 90% sequence homology among members in the group. The group II subunits (A3 B4, A5A4B3) exhibit a similar level of homology among themselves, although they contain less methionine and are larger (Mr ″ 62,000–69,000) than group I subunits. Sequence homology between a member of one group and a member of the other is only 60–70%. Since the sulfur amino acid content of subunits is variable and genetic polymorphism in subunit composition has been documented, alteration of the functional and nutritional properties of these seed proteins by genetic manipulation may be possible.

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Authors and Affiliations

  1. USDA/ARS Agronomy Department, Purdue University, 47907, West Lafayette, IN

    Niels C. Nielsen

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Nielsen, N.C. The structure and complexity of the 11S polypeptides in soybeans. J Am Oil Chem Soc 62, 1680–1686 (1985). https://doi.org/10.1007/BF02541665

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  • DOI: https://doi.org/10.1007/BF02541665

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