Characterization of the Co2+ and Ni2+ binding amino‐acid residues of the N‐terminus of human albumin

摘要: Patients suffering from myocardial ischemia reportedly exhibit reduced in vitro binding of exogenous Co2+ to the N-terminal human serum albumin (HSA). The purpose our investigation was simulate changes N-terminus HSA that may account for these ischemia-induced modifications cobalt site. HPLC, LC-MS and 1H NMR analyses have shown region Asp-Ala-His-Lys binds transition metals Ni2+. Synthetic peptides with first 2–12 amino acids sequence demonstrated three acids, Asp-Ala-His, are essential strong cobalt. Modification peptide by way N-acetylation or deletion one more acid resulted no Because degradation susceptible, specific metal site decreased observed during ischemic events, an assay detects this could be useful diagnosis ischemia.