2006/06/29 by Asami Kawakami, Kazuyuki Kubota, Naoyuki Yamada +5 · 1 citation
Biochemistry, Genetics and Molecular Biology · Chemistry · Medicine · #Albumin #Biochemistry #Chemistry #Cysteine #Enzyme #Hemoglobin structure and function #Human serum albumin #Methemoglobinemia and Tumor Lysis Syndrome #Protein Interaction Studies and Fluorescence Analysis #Serum albumin #Thiol
paper · doi:10.1111/j.1742-4658.2006.05341.x
openalex publication_date 2006/06/29 · openalex created_date 2016/06/24 · openalex updated_date 2026/06/22
Human serum albumin (HSA) exists in both reduced and oxidized forms, and the percentage of oxidized albumin increases in several diseases. However, little is known regarding the pathophysiological significance of oxidation due to poor characterization of the precise structural and functional properties of oxidized HSA. Here, we characterize both the structural and functional differences between reduced and oxidized HSA. Using LC-ESI-TOFMS and FTMS analysis, we determined that the major structural change in oxidized HSA in healthy human plasma is a disulfide-bonded cysteine at the thiol of Cys34 of reduced HSA. Based on this structural information, we prepared standard samples of purified HSA, e.g. nonoxidized (intact purified HSA which mainly exists in reduced form), mildly oxidized and highly oxidized HSA. Using these standards, we demonstrated several differences in functional properties of HSA including protease susceptibility, ligand-binding affinity and antioxidant activity. From these observations, we conclude that an increased level of oxidized HSA may impair HSA function in a number of pathological conditions.