Structural changes accompanying human serum albumin's binding of fatty acids are concerted.

Long chain fatty acids (LCFAs), a major source of cellular energy, are solubilized and transported in the blood by binding to serum albumin. Changes in human serum albumin's (HSA's) UV absorption and characteristic reactivity with pyridoxal-5'-phosphate appear to reflect a concerted change in its structure upon binding five equivalents of myristate. Isothermal titrations with myristate and other LCFA anions are also consistent with the presence of five strong, interacting, binding sites.

Reactions of acrylamide with glutathione and serum albumin.

Rate constants of 0.0054 and 0.021 M(-1)s(-1) for the reactions of acrylamide with human serum albumin (HSA) and glutathione (GSH), respectively, were determined under physiological conditions by following the loss of their thiol groups in the presence of excess acrylamide.