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Volumn 445, Issue 1, 2006, Pages 19-25

Disulfide between Cys392 and Cys438 of human serum albumin is redox-active, which is responsible for the thioredoxin-supported lipid peroxidase activity

(2) Cha, Mee Kyung a Kim, Il Han a

a PaiChai University (South Korea)

Author keywords

Antioxidative function of human serum albumin; Human blood; Lipid peroxidase activity; Redox active disulfide; Thioredoxin; Thioredoxin linked peroxidase

Indexed keywords

CYSTEIN392; CYSTEIN438; CYSTEINE; DISULFIDE; HUMAN SERUM ALBUMIN; LEUCINE; LIPID HYDROPEROXIDE; LIPID PEROXIDASE; PROLINE; THIOREDOXIN; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ARTICLE; BLOOD; CATALYSIS; CHEMICAL MODIFICATION; DISULFIDE BOND; ELECTRON; ENZYME ACTIVITY; HUMAN; LIPID HYDROLYSIS; LIPID PEROXIDATION; OXIDATION REDUCTION REACTION; PEPTIDE ANALYSIS; PRIORITY JOURNAL;

BINDING SITES; CATALYSIS; CYSTEINE; DISULFIDES; HUMANS; LIPID PEROXIDATION; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; PEROXIDASES; SERUM ALBUMIN; THIOREDOXIN;

EID: 29244471692 PISSN: 00039861 EISSN: 10960384 Source Type: Journal
DOI: 10.1016/j.abb.2005.09.022 Document Type: Article

Times cited : (22)

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