The modification of structural and functional properties of human hemoglobin induced by nitroglycerin under different oxygen regime conditions

   
Artyukhov V.G.1, Kalaeva E.A.1 , Putintseva O.V.1, Polyubez'eva A.I.1

1. Voronezh State University, Voronezh, Russia
Section: Experimental Study
DOI: 10.18097/PBMC20166203251      PubMed Id: 27420615
Year: 2016  Volume: 62  Issue: 3  Pages: 251-258
Human oxyhemoglobin exhibits high resistance to nitroglycerin during incubation of the protein with this compound for 0.3-3 h. Prolonged exposure (24 h) leads to activation of methemoglobin production. In the presence of nitroglycerin hemoglobin molecules undergo rapid oxidation during deoxygenation with formation of methemoglobin as the terminal product of human oxyhemoglobin interaction with nitroglycerin. The scheme of interaction processes of oxyhemoglobin with nitroglycerin in different conditions of oxygen regime is proposed. Partially deliganded hemoglobin plays the leading role in the initiation of hemoglobin oxidation processes.
Download PDF:  
Keywords: hemoglobin, oxygen-binding properties, oxyhemoglobin dissociation curve, nitroglycerin, nitric oxide, electron absorption spectrum
Citation:

Artyukhov, V. G., Kalaeva, E. A., Putintseva, O. V., Polyubez'eva, A. I. (2016). The modification of structural and functional properties of human hemoglobin induced by nitroglycerin under different oxygen regime conditions. Biomeditsinskaya Khimiya, 62(3), 251-258.
References  
 2024 (vol 70)
 2023 (vol 69)
 2022 (vol 68)
 2021 (vol 67)
 2020 (vol 66)
 2019 (vol 65)
 2018 (vol 64)
 2017 (vol 63)
 2016 (vol 62)
 2015 (vol 61)
 2014 (vol 60)
 2013 (vol 59)
 2012 (vol 58)
 2011 (vol 57)
 2010 (vol 56)
 2009 (vol 55)
 2008 (vol 54)
 2007 (vol 53)
 2006 (vol 52)
 2005 (vol 51)
 2004 (vol 50)
 2003 (vol 49)