Studies on the cold-insoluble fraction of the water-extractable soybean proteins. II. Factors influencing conformation changes in the 11 S component
作者： W.J. Wolf , D.R. Briggs
DOI: 10.1016/0003-9861(58)90163-2
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摘要: Abstract Ultracentrifugal studies indicate that the 11 S globulin of soybeans is capable undergoing conformation changes probably involving dissociation into subunits which appear to be one-half and approximately one-eighth size molecule. These occur at low ionic strength alkaline pH values, moderate strengths acid in presence sodium octylbenzene sulfonate relatively concentrations urea. The generated are reversible on increasing strength. Those by detergent also removal an increase neutral pH. Conformation forms protein pH, or higher detergent, while similar sedimenting properties those (above) exhibiting reversibility, irreversible.
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