Alain Chevalier1, Didier Guillochon, Naïma Nedjar, Jean-Marie Piot, Mokambes Waran Vijayalakshmi, Daniel Thomas
1Laboratoire de biophysique, Centre hospitalier universitaire Necker, Paris, France.
Tóm tắt
Glutaraldehyde is a widely used reagent for hemoglobin cross-linking in blood substitutes research. However, hemoglobin polymerization by glutaraldehyde involves modifications of its functional properties, such as oxygen affinity, redox potentials, and autoxidation kinetics. The aim of this article is to investigate, by electron paramagnetic resonance and Mossbauer spectroscopies, the changes that occur in the iron environment after glutaraldehyde cross-linking. Spectrometric studies were performed with native hemoglobin and hemoglobin cross-linked as soluble and insoluble polymers. Spectrometry data comparison with glutaraldehyde-modified hemoglobin functional properties allows to interpret from a structural point of view that glutaraldehyde action occurs as a decrease of the O—N(F8His) distance, an increase of the Fe—N(F8His) bond length, and the decrease of the distal-side steric hindrance.Key words: hemoglobin, glutaraldehyde, Mossbauer spectroscopy, electron paramagnetic resonance, blood substitute.
