Cys34 Adducts of Reactive Oxygen Species in Human Serum Albumin
نویسندگان
چکیده
منابع مشابه
Enrichment of cysteinyl adducts of human serum albumin.
We report a method to enrich cysteinyl adducts of human serum albumin (HSA), representing biomarkers of exposure to systemic electrophiles. Because the major site of HSA adduction is the single free sulfhydryl group at Cys34, we used thiol-affinity resins to remove mercaptalbumin (i.e., unadducted HSA) from the cysteinyl adducts. Electrospray ionization mass spectrometry was used to detect merc...
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The degree of oxidized cysteine (Cys) 34 in human serum albumin (HSA), as determined by high performance liquid chromatography (HPLC), is correlated with oxidative stress related pathological conditions. In order to further characterize the oxidation of Cys34-HSA at the molecular level and to develop a suitable analytical method for a rapid and sensitive clinical laboratory analysis, the use of...
متن کاملHuman Serum Albumin Cys34 Oxidative Modifications following Infiltration in the Carotid Atherosclerotic Plaque
OBJECTIVES To evaluate if the prooxidant environment present in atherosclerotic plaque may oxidatively modify filtered albumin. METHODS Fluorescein-5-maleimide labelled plasma samples and plaque extracts from 27 patients who had undergone carotid endarterectomy were analysed through nonreducing SDS-PAGE for albumin-Cys(34) oxidation. Furthermore, degree and pattern of S-thiolation in both cir...
متن کاملCross-talk between Cys34 and lysine residues in human serum albumin revealed by N-homocysteinylation.
Protein N-homocysteinylation involves a post-translational modification by homocysteine (Hcy)-thiolactone. In humans, about 70% of circulating Hcy is N-linked to blood proteins, mostly to hemoglobin and albumin. It was unclear what protein site(s) were prone to Hcy attachment and how N-linked Hcy affected protein function. Here we show that Lys(525) is a predominant site of N-homocysteinylation...
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ژورنال
عنوان ژورنال: Chemical Research in Toxicology
سال: 2012
ISSN: 0893-228X,1520-5010
DOI: 10.1021/tx300096a