ArticlePloS one2017
Modifications of hemoglobin and myoglobin by Maillard reaction products (MRPs).
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 21 citations in OpenAlex.
- D-galactose enhances Maillard reaction and antioxidant activity of arginine-derived products: experimental and molecular insights.Frontiers in nutrition · 2026Article
- Poly(vinyl chloride) microplastics induce structural and functional alterations in myoglobin.RSC advances · 2025Article
- Probing hemoglobin glyco-products by fluorescence spectroscopy.RSC advances · 2019Article
- Myocardial native-T1 times are elevated as a function of hypertrophy, HbA1c, and heart rate in diabetic adults without diffuse fibrosis.Magnetic resonance imaging · 2019Article
- The relationship between plasma amino acids and circulating albumin and haemoglobin in postabsorptive stroke patients.PloS one · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High performance liquid chromatography (HPLC) coupled with a Fraction Collector was employed to isolate Maillard reaction products (MRPs) formed in model systems comprising of asparagine and monosaccharides in the 60-180°C range. The primary MRP which is detected at 60°C is important for Acrylamide content and color/aroma development in foods and also in the field of food biotechnology for controlling the extent of the Maillard reaction with temperature. The discrete fractions of the reaction products were reacted with Hemoglobin (Hb) and Myoglobin (Mb) at physiological conditions and the reaction adducts were monitored by UV-vis and Attenuated Total Reflection-Fourier transform infrared (FTIR) spectrophotometry. The UV-vis kinetic profiles revealed the formation of a Soret transition characteristic of a low-spin six-coordinated species and the ATR-FTIR spectrum of the Hb-MRP and Mb-MRP fractions showed modifications in the protein Amide I and II vibrations. The UV-vis and the FTIR spectra of the Hb-MRPs indicate that the six-coordinated species is a hemichrome in which the distal E7 Histidine is coordinated to the heme Fe and blocks irreversibly the ligand binding site. Although the Mb-MRPs complex is a six-coordinated species, the 1608 cm-1 FTIR band characteristic of a hemichrome was not observed.
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