ArticleMolecular pharmaceutics2013
Metal-catalyzed oxidation of protein methionine residues in human parathyroid hormone (1-34): formation of homocysteine and a novel methionine-dependent hydrolysis reaction.
Article in Molecular pharmaceutics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- Near UV and Visible Light-Induced Degradation of IgG2: Photo-Fenton Reaction in Citrate Buffer.Pharmaceutical research · 2026Article
- Designing Formulation Strategies for Enhanced Stability of Therapeutic Peptides in Aqueous Solutions: A Review.Pharmaceutics · 2023Review
- Identifying a role for the interaction of homocysteine and copper in promoting cardiovascular-related damage.Amino acids · 2021Article
- A Comprehensive Assessment of All-Oleate Polysorbate 80: Free Fatty Acid Particle Formation, Interfacial Protection and Oxidative Degradation.Pharmaceutical research · 2021Article
- Effect of Iron Oxide Nanoparticles on the Oxidation and Secondary Structure of Growth Hormone.Journal of pharmaceutical sciences · 2019Article
- Demethylation of methionine and keratin damage in human hair.Amino acids · 2018Article
- An Efficient and Rapid Method to Monitor the Oxidative Degradation of Protein Pharmaceuticals: Probing Tyrosine Oxidation with Fluorogenic Derivatization.Pharmaceutical research · 2017Article
- Oxidation of therapeutic proteins and peptides: structural and biological consequences.Pharmaceutical research · 2014Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The oxidation of PTH(1-34) catalyzed by ferrous ethylenediaminetetraacetic acid (EDTA) is site-specific. The oxidation of PTH(1-34) is localized primarily to the residues Met[8] and His[9]. Beyond the transformation of Met[8] and His[9] into methionine sulfoxide and 2-oxo-histidine, respectively, we observed a hydrolytic cleavage between Met[8] and His[9]. This hydrolysis requires the presence of Fe(II) and oxygen and can be prevented by diethylenetriaminepentaacetic acid (DTPA) and phosphate buffer. Conditions leading to this site-specific hydrolysis also promote the transformation of Met[8] into homocysteine, indicating that the hydrolysis and transformation of homocysteine may proceed through a common intermediate.
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Registered trials
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