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. 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