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Comparison of acid‐induced conformation changes between 7S and 11S globulin in soybean seeds
Author(s) -
Koshiyama I.
Publication year - 1972
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740230706
Subject(s) - optical rotatory dispersion , chemistry , denaturation (fissile materials) , ultracentrifuge , globulin , dissociation (chemistry) , ionic strength , sodium , bivalent (engine) , biochemistry , chromatography , circular dichroism , biology , nuclear chemistry , organic chemistry , aqueous solution , metal , immunology
The acid‐induced conformation changes between 7 and 11 S globulin, the major storage proteins in soybean seeds, were compared by ultraviolet difference spectra, ultracentrifugation and optical rotatory dispersion. Maximum denaturation occurred at approximately pH 2 in both and dissociation of the proteins into subunits and unfolding of the polypeptide chains were observed simultaneously. However, both proteins showed apparent differences in their readiness to undergo acid‐induced denaturation. The differences were particularly remarkable in the presence of 0.1 ionic strength sodium chloride.