The method of differential scanning microcalorimetry was employed to study the effect of NaCl, KCl and (NH4)2SO4 on the stability of 11S globulins from soy beans and vicia faba at pH 7.6. The temperature and enthalpy of denaturation were found to rise in a non‐linear way with increase of salt concentration. According to the efficiency of the increase in denaturation temperature the salts under study can be arranged in the series (NH4)2SO4 > NaCl = KCl. The dependences of excess free energy of denaturation per protomer of 11S globulins on salt concentration at 293 and 352 K were determined. These dependences are described within the scope of a two‐state model with allowance made for the contributions of electrostatic and lyotropic effects.
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Danilenko et al. (1986) studied this question.
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