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Open AccessJournal ArticleDOI

The thiol pool in human plasma: the central contribution of albumin to redox processes.

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TLDR
A critical review of the plasma thiol pool is provided with a focus on human serum albumin, an important target for oxidants and electrophiles due to its reactivity with a wide variety of species and its relatively high concentration.
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This article is published in Free Radical Biology and Medicine.The article was published on 2013-12-01 and is currently open access. It has received 519 citations till now. The article focuses on the topics: Human serum albumin & Thiol.

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Citations
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Sulfenic acid in human serum albumin: Reaction with thiols, oxidation and spontaneous decay.

TL;DR: In this article, the sulfenic acid (SSA)-SOH reaction with a thiol leading to the formation of a mixed disulfide was investigated and the reaction occurred through a concerted or direct displacement mechanism with the thiolate (RS−) as nucleophile towards HSA-SOH.
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Black phosphorus quantum dots are useful oxidase mimics for colorimetric determination of biothiols

TL;DR: This work discovers a useful oxidase mimics but also sets up a reliable platform based on BP QDs in colorimetric detection of glutathione and cysteine in pharmaceutical preparations.
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An investigation of thiol/disulfide homeostasis and ischemia-modified albumin levels to assess the oxidative stress in dogs with canine distemper.

TL;DR: Investigation of the diagnostic value of thiol/disulfide homeostasis (TDH) and ischemia-modified albumin (IMA) levels in evaluating oxidative stress in dogs with canine distemper found IMA was superior.
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Characterization of the complex between native and reduced bovine serum albumin with aquacobalamin and evidence of dual tetrapyrrole binding.

TL;DR: Investigation of the reaction between aquacobalamin and bovine serum albumin using Ultraviolet–Visible and fluorescent spectroscopy, and electron paramagnetic resonance suggests that the two tetrapyrroles interact with BSA in different binding pockets.
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Quantitation of Oxidative Modifications of Commercial Human Albumin for Clinical Use: Thiol Oxidation and Carbonylation.

TL;DR: Commercial HSA products for clinical use have a more thermally stable state and remain in a helix-rich structure, even though their specific amino acids (mainly Cys and Lys residues) are oxidatively modified.
References
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Journal ArticleDOI

Bilirubin is an antioxidant of possible physiological importance

TL;DR: The data support the idea of a "beneficial" role for bilirubin as a physiological, chain-breaking antioxidant.
Book

All About Albumin: Biochemistry, Genetics, and Medical Applications

TL;DR: The Albumin Molecule: Its Structure and Chemical Properties and Practical Aspects: Albumin in the Laboratory.
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Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide.

TL;DR: Peroxynitrite anion was a less effective thiol-oxidizing agent than its anion, with oxidation presumably mediated by the decomposition products, hydroxyl radical and nitrogen dioxide.
Journal ArticleDOI

Homocysteine and Cardiovascular Disease

TL;DR: In this article, an elevated level of total homocysteine (tHcy) in blood, denoted hyperhomocysteinemia, is emerging as a prevalent and strong risk factor for atherosclerotic vascular disease in the coronary, cerebral, and peripheral vessels, and for arterial and venous thromboembolism.
Journal ArticleDOI

Albumin as a drug carrier: design of prodrugs, drug conjugates and nanoparticles.

TL;DR: This review gives an account of the different drug delivery systems which make use of albumin as a drug carrier with a focus on those systems that have reached an advanced stage of preclinical evaluation or that have entered clinical trials.
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