RESUMO
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. Although HSA is usually thought to have many independent LCFA anion binding sites, just five interacting sites appear to account for the changes in structure that accompany its binding of myristate.
Assuntos
Ácidos Graxos/química , Albumina Sérica/química , Sítios de Ligação , Calorimetria , Humanos , Ácido Mirístico/química , Conformação Proteica , Fosfato de Piridoxal/química , Espectrofotometria UltravioletaRESUMO
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. Based on these in vitro values, reactions with these thiols appear to account for most of acrylamide's elimination from the body. Combined with data from other studies, these results should be useful for assessing the health risk of dietary acrylamide.
