Modification of amino acid residues in human serum albumin by myeloperoxidase.

Myeloperoxidase is released from stimulated polymorphonuclear leukocytes at inflammatory loci. Besides its bactericidal activity, it interacts with human serum albumin that is essential for the endothelial uptake of myeloperoxidase and its contribution in regulation of the blood vessel tonus. Here, we investigated which kinds of modification dominate in the albumin protein by the myeloperoxidase-hydrogen peroxide system at physiological pH.