Abstract
Background: Hemoglobin (Hb), oxygen, carbon dioxide, and electron transporter of the body, may enter to an oxidation process that can convert oxyhemoglobin (oxyHb) to methemoglobin (metHb) and hemichrome. Surfactants can facilitate oxidation process that may accumulate hemichrome in red blood cells. Methods: In the present study, the interaction of purified Hb with sodium dodecyl sulfate (SDS, 0-5 mM) and ascorbic acid (AA, 0-5 mM) was evaluated by UV-Vis spectroscopy and multivariate curve resolution techniques. Results: Reconstructed spectral and concentration profiles showed three forms of Hb name as oxyHb, metHb, and hemichrome with lack of fit values less than 1.85%. AA hindered the oxidation process of Hb. Conclusion: A decrease in critical micelle concentration of SDS in the presence of AA and interaction of AA with hydrogen peroxide, which is produced during the interaction of Hb with SDS, are two reasons for diminution in the oxidation process of Hb when accompanied with AA.
Highlights
Hemoglobin (Hb), oxygen, carbon dioxide, and electron transporter of the body, may enter to an oxidation process that can convert oxyhemoglobin to methemoglobin and hemichrome
The results showed that Multivariate curve resolution alternative least squares (MCR-ALS) was an adequate technique for the estimation of concentration and spectral profiles of Hb-denatured products upon interaction with dodecyl trimethylammonium bromide (DTAB)
UV-Vis Spectra The spectroscopy is a well-adopted tool to study the changes in protein conformation upon binding with surfactants [26]
Summary
Hemoglobin (Hb), oxygen, carbon dioxide, and electron transporter of the body, may enter to an oxidation process that can convert oxyhemoglobin (oxyHb) to methemoglobin (metHb) and hemichrome. Surfactants can facilitate oxidation process that may accumulate hemichrome in red blood cells. Methods: In the present study, the interaction of purified Hb with sodium dodecyl sulfate (SDS, 0-5 mM) and ascorbic acid (AA, 0-5 mM) was evaluated by UV-Vis spectroscopy and multivariate curve resolution techniques. Hemoglobin (Hb) is the major hemeprotein of the red blood cells which is responsible for the transport of oxygen and carbon dioxide, hydrogen peroxide (H2O2) dispersion, and electron transportation to all organs, as well as regulation of blood pH [1]. The study of surfactant-protein interactions is of great importance, theoretically and practically [6]
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