ArticleAnalytical letters
A Robust Analytical Approach for the Identification of Specific Protein Carbonylation Sites: Metal-Catalyzed Oxidations of Human Serum Albumin.
Article in Analytical letters. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 7 citations in OpenAlex.
- Investigation of the Immunogenic Properties of Ovalbumin Modified by Urban Airborne Particulate Matter.Archivum immunologiae et therapiae experimentalis · 2023Article
- Differentiating the Effects of Oxidative Stress Tests on Biopharmaceuticals.Pharmaceutical research · 2019Article
- Metal-catalyzed oxidation of human serum albumin does not alter the interactive binding to the two principal drug binding sites.Biochemistry and biophysics reports · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The formation of protein carbonyls in the metal-catalyzed oxidation of human serum albumin (HSA) is characterized using a new analytical approach that involves tagging the modification site with multiple hydrazide reagents. Protein carbonyl formation at lysine and arginine residues was catalyzed with copper and iron ions, and the resulting oxidation patterns in HSA are contrasted. A total of 18 modification sites were identified with iron ion catalysis and 14 with copper ion catalysis. However, with the more stringent requirement of identification with at least two tagging reagents, the number of validated modification sites drops to 10 for iron and 9 for copper. Of the 14 total validated sites, there were only five in common for the two metal ions. The results illustrate the value of using multiple tagging agents and highlight the selective and specific nature of metal-catalyzed protein oxidations.
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Registered trials
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