Comparison of the primary structure of the acidic polypeptides of glycinin

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Abstract

Some essential features of the primary structures of five acidic polypeptides from the major 11 S soybean storage protein were studied. Each purified polypeptide was cleaved at methionine using cyanogen bromide, and then each resulting fragment was purified. A comparison of the NH2-terminal amino acid sequences of each fragment, coupled with an identification of both the carboxyl and amino terminal fragments, permitted ordering of the fragments along the polypeptides. It was found that the five acidic polypeptides were synthesized at the direction of a family of homologous genes. Evidence was also obtained which suggested that there were repeated domains of amino acid sequence within each of the five molecules. © 1981.

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Moreira, M. A., Hermodson, M. A., Larkins, B. A., & Nielsen, N. C. (1981). Comparison of the primary structure of the acidic polypeptides of glycinin. Archives of Biochemistry and Biophysics, 210(2), 633–642. https://doi.org/10.1016/0003-9861(81)90230-7

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