ArticleIranian biomedical journal2011
Kinetic investigation of myeloperoxidase upon interaction with copper, cadmium, and lead ions.
Article in Iranian biomedical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 3 citations in OpenAlex.
- Elemental analysis in menstrual effluent of women with PCOS: association with oxidative stress mechanisms: a case-control study.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Article
- Faecal Myeloperoxidase as a Biomarker of Endoscopic Activity in Inflammatory Bowel Disease.Journal of Crohn's & colitis · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMyeloperoxidase (MPO), which is abundantly expressed in neutrophils, catalyzes the formation of a number of reactive oxidant species. However, evidence has emerged that MPO-derived oxidants contribute to tissue damage and initiation and propagation of inflammatory diseases, particularly, cardiovascular diseases. Therefore, studying the regulatory mechanisms of the enzyme activity is of great importance. For clarifying some possible mechanism of the enzyme activity, kinetic investigations of MPO in the presence of Copper (Cu), Cadmium (Cd), and Lead (Pb) ions were carried out in vitro.
methodsMPO was partially purified from human white blood cells using ion-exchange and gel-filtration chromatography techniques. Its activity was measured spectrophotometrically by using tetramethyl benzidine (TMB) as substrate.
resultsPurified enzyme had a specific activity of 21.7 U/mg protein with a purity index of about 0.71. Cu inhibited MPO activity progressively up to a concentration of 60 mM at which about 80% of inhibition achieved. The inhibition was non-competitive with respect to TMB. An inhibitory constant (Ki) of about 19 mM was calculated from the slope of repot. Cd and Pb did not show any significant inhibitory effect on the enzyme activity.
conclusionThe results of the present study may indicate that there are some places on the enzyme and enzyme-substrate complex for Cu ions. Binding of Cu ions to these places result in conformational changes of the enzyme and thus, enzyme inhibition. This inhibitory effect of Cu on the enzyme activity might be considered as a regulatory mechanism on MPO activity.
Indexed as
Identifiers
21987117PMC3639747W2115293744What OpenQuestion holds
Registered trials
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