albumin - publications

Predict more albumin - ligand interactions now!

1. IUBMB Life. 2012 Feb 20. doi: 10.1002/iub.567. [Epub ahead of print]

Quantitative evaluation of the role of cysteine and methionine residues in the
antioxidant activity of human serum albumin using recombinant mutants.

Iwao Y, Ishima Y, Yamada J, Noguchi T, Kragh-Hansen U, Mera K, Honda D, Suenaga
A, Maruyama T, Otagiri M.

Department of Biopharmaceutics, Graduate School of Pharmaceutical Sciences,
Kumamoto University, Kumamoto, Japan; Department of Pharmaceutical Engineering,
School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Japan.

The importance of cysteine (Cys) and methionine (Met) residues for the
antioxidant activity of human serum albumin (HSA) was investigated using
recombinant HSA mutants, in which Cys34 and/or the six Met residues had been
mutated to Ala. The scavenging activities of the mutants against five reactive
oxygen and nitrogen species were evaluated by a chemiluminescence assay, electron
paramagnetic resonance spectroscopy, or a HPLC-flow reactor assay. Our results
showed that the contributions of Cys34 and the Met residues to the antioxidant
activity of HSA were 61% and 29% against O(2) (•-) , 68% and 61% against H(2)
O(2) , 38% and 6% against HO(•) , 36% and 13% against HOCl, and 51% and 1%
against (•) NO, respectively. Thus, the findings propose in a direct way that
Cys34 plays a more important role than the Met residues in the antioxidant
activity of HSA. © 2012 IUBMB IUBMB Life, 2012.

Copyright © 2012 Wiley Periodicals, Inc.

PMID: 22351593 [PubMed - as supplied by publisher]