Journal ArticleDOI
Mass spectrometric identification of modifications to human serum albumin treated with hydrogen peroxide
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TLDR
The data presented here for human serum albumin demonstrate the utility of mass spectrometry in studying protein alterations and may be helpful in assessing the ability of proteins to act as antioxidants in biological systems which are subject to oxidant stress as in cases of inflammation and in the aging process.About:
This article is published in Archives of Biochemistry and Biophysics.The article was published on 1993-09-01. It has received 53 citations till now. The article focuses on the topics: Human serum albumin & Albumin.read more
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Journal ArticleDOI
Characterization of drugs as antioxidant prophylactics
TL;DR: The current evidence to support the notion that drugs for a particular therapeutic category might possess useful antioxidant capacity hence minimising tissue injury due to free radicals is examined.
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Age-related change in redox state of human serum albumin.
TL;DR: In healthy elderly subjects, f−(HMA) was significantly lower than in healthy young male subjects, indicating that HSA in the elderly becomes more oxidized than in the young subjects, thus securing a certain redox buffer capacity with age.
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Effect of Oxidative Stress on the Structure and Function of Human Serum Albumin
TL;DR: Mild oxidation of HSA has no detectable effect on the binding of drugs to site I in subdomain IIA and both the ligand binding property of site II and the esterase–like activity of oxidized HSAs are decreased, most probably due to conformational changes in sub domain IIIA.
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Intravenous iron administration induces oxidation of serum albumin in hemodialysis patients.
Makoto Anraku,Kenichiro Kitamura,Ayumi Shinohara,Masataka Adachi,Ayaka Suenaga,Toru Maruyama,Kei Miyanaka,Taku Miyoshi,Naoki Shiraishi,Hiroshi Nonoguchi,Masaki Otagiri,Kimio Tomita +11 more
TL;DR: The results of this study indicate that the HPLC analysis of serum albumin represents a potentially useful method for the quantitative and qualitative evaluation of oxidative stress in HD patients, and strongly suggest the possibility that oxidative stress, generated by IVIR, enhances the oxidation of albumin in those patients.
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Post-translational Modifications and Mass Spectrometry Detection
TL;DR: This review analyzed all the PTM data introduced in the Universal Protein Resource (UniProt) and the literature published in the last three years to ascertain the state of the art in mass spectrometry and proteomics methodologies for the study of PTMs.