The Interaction of Hemoglobin With Sodium Dodecyl Sulfate in Presence of Ascorbic Acid

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....

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Radnoosh Mirzajani, Ebrahim Mirzajani, Heshmatollah Ebrahimi-Najafabadi
Formato: article
Lenguaje:EN
Publicado: Hamadan University of Medical Sciences 2020
Materias:
Acceso en línea:https://doaj.org/article/1de293c842d54016977bd321c916bc78
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
Descripción
Sumario: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.