Abstract
Generalized 2D correlation spectroscopy (COS) has been applied to FTIR spectra of porcine plasma proteins to elucidate the sequence of events leading to pH- and/or thermal-induced protein unfolding and aggregation. Changes in the amide I′ region of the infrared spectra (in the pH range between 7.5 and 4.5, at 0.5 pH intervals) at 30 °C were especially evident as the pH approached the p I of serum albumin (4.8), with the globulin fraction in the plasma proteins undergoing denaturation prior to serum albumin. The effect of increasing temperature (from 30 to 90 °C, in increments of 5 °C) on the secondary structure of the plasma proteins at pHs in the range of 7.5–6.0 revealed that a decrease in alpha-helical structures is taken place previously to diminish native beta-sheets. So, the overall results of this study demonstrate that serum albumin and the globulin fraction differ in their sensitivity to pH and temperature.
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