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Seyed M, Gholam R, Mahmood K, Hadi A, Naghmeh S, Ahmad S, Shahrokh
S, Faizan A and Ali M. 2009. Effects of mobile phone radiofrequency on the
structure and function of the normal human hemoglobin. International Journal of
Biological Macromolecules 44(3):278-285.

       Hemoglobin is a protein whose physiological function is to transport
oxygen from the lungs to the tissues. Seyed at el. investigated the
effects of mobile phone radiofrequency (910 MHz and 940 MHz) on the
structure and function of hemoglobin (HbA). Oxygen affinity was measured
by using sodium dithionite with Ultraviolet–visible spectrophotometer.
Structural changes were studied by circular dichroism (characterizes
protein structure) and fluorescence spectroscopy. It was found that mobile
phone electromagnetic fields (EMFs) altered oxygen affinity and the
tertiary structure of HbA. It was found that HbA binded less oxygen in the
lungs and released more oxygen than normal to the tissues. This finding
suggests that exposure to electromagnetic fields could affect human’s
normal respiration. The decrease of oxygen affinity of HbA corresponded
to the EMFs intensity and time of exposure.

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Annotated bibliography #3

  • 1. Seyed M, Gholam R, Mahmood K, Hadi A, Naghmeh S, Ahmad S, Shahrokh S, Faizan A and Ali M. 2009. Effects of mobile phone radiofrequency on the structure and function of the normal human hemoglobin. International Journal of Biological Macromolecules 44(3):278-285. Hemoglobin is a protein whose physiological function is to transport oxygen from the lungs to the tissues. Seyed at el. investigated the effects of mobile phone radiofrequency (910 MHz and 940 MHz) on the structure and function of hemoglobin (HbA). Oxygen affinity was measured by using sodium dithionite with Ultraviolet–visible spectrophotometer. Structural changes were studied by circular dichroism (characterizes protein structure) and fluorescence spectroscopy. It was found that mobile phone electromagnetic fields (EMFs) altered oxygen affinity and the tertiary structure of HbA. It was found that HbA binded less oxygen in the lungs and released more oxygen than normal to the tissues. This finding suggests that exposure to electromagnetic fields could affect human’s normal respiration. The decrease of oxygen affinity of HbA corresponded to the EMFs intensity and time of exposure.