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Compositional relationships among electrophoretic isolates from cottonseed gossypium hirsutum cultivar deltapine 16 protein bodies



Compositional relationships among electrophoretic isolates from cottonseed gossypium hirsutum cultivar deltapine 16 protein bodies



Phytochemistry 19(8): 1647-1652



Minor differences exist among polypeptides isolated from cottonseed storage globulins with respect to nutritionally-limiting amino acids, although the composition of most isolates closely resembles that of the entire storage globulin fraction. Glutamate, arginine and aspartate are the most abundant amino acids; cysteine and methionine are the least abundant. In contrast to the 10 polypeptide bands in the SDS-PAGE [sodium dodecyl sulfate polyacrylimide gel electrophoresis] pattern, isoelectric focusing produced a pattern of 49 components within a range of pH 4.5-9.5. A 2-dimensional electrophoretic separation indicated that most of the polypetides resolved by SDS-PAGE are heterogeneous with respect to charge. The high ratio of isoelectric to molecular weight forms may prove advantageous for efforts to genetically improve the quality of cottonseed protein for use as food.

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Accession: 005024066

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