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Electrophoretic study of heterogeneity of the salt soluble fraction of cottonseed proteins


, : Electrophoretic study of heterogeneity of the salt soluble fraction of cottonseed proteins. Biokhimiya 50(6): 1030-1038

A modified procedure for selective isolation of the globulin fraction from cotton seeds is described. The heterogeneity of the polypeptide patterns of globulins was studied by SDS polyacrylamide gel electrophoresis in the acrylamide density gradient of 4-20% and 10-17%. This procedure resulted in good separation of proteins with apparent molecular weights ranging from 11 to 21 kD. Some cotton breeds were compared by two-dimensional electrophoresis performed according to O'Farrel and were found to differ by individual peptide spots. The data obtained suggest the existence of intraspecific polymorphism of the globulin fraction of storage proteins from cotton seeds, as well as of well-defined interspecific differences in the composition of these proteins.

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Related references

Chugunova, E.; Odintsova, T.; Egorov, T.; Sozinov, A., 1985: Electrophoretic investigation of the heterogeneity of the salt-soluble fraction of cottonseed proteins. Biochemistry 50(2): 873-881

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