The most abundant plasma protein, human serum albumin (HSA), plays a key part in the body’s antioxidant defense against reactive species [1]. This study was aimed at correlating oxidant-induced chemical and structural effects on HSA [2].
Human Serum Albumin (HSA), the most abundant protein of body fluids, has a “modular” three-domain structure potentially responding to stress by means of changes of conformation (1). Besides acting as the main carrier protein of the circulation, HSA is also an obvious target of extracellular reactive oxidant species due to its high abundance in plasma. It is for this reason considered the main anti-oxidant defense in blood (2).
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