Effects of mobile phone radiofrequency on the structure and function of the normal human hemoglobin med./bio.

[Wirkungen von Mobiltelefon-Hochfrequenz auf die Struktur und Funktion normalen menschlichen Hämoglobins]

Ziel der Studie (lt. Autor)

Endpunkt

• Struktur und Funktion von Hämoglobin

Exposition/Befeldung (teilweise nur auf Englisch)

• • Hochfrequenz
• • CW (kontinuierliche Welle)
  • Mobilfunk
  • Mobiltelefon

Vollständige Ansicht Kompaktansicht

Methoden Endpunkt/Messparameter/Methodik

• Struktur und Funktion von Hämoglobin (Zirkular-Dichroismus, Fluoreszenz-Spektroskopie, Sauerstoff-Affinität (Spektrophotometrie), Messungen der Fluoreszenz, Aggregation und thermischen Denaturierung)

Hauptergebnis der Studie (lt. Autor)

Studie gefördert durch

• Iran National Science Foundation (INSF)
• University of Tehran, Iran

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• Damm M et al. (2012): Can electromagnetic fields influence the structure and enzymatic digest of proteins? A critical evaluation of microwave-assisted proteomics protocols
• Magazu S et al. (2010): FTIR spectroscopy studies on the bioprotective effectiveness of trehalose on human hemoglobin aqueous solutions under 50 Hz electromagnetic field exposure
• George DF et al. (2008): Non-Thermal effects in the microwave induced unfolding of proteins observed by chaperone binding
• Copty AB et al. (2006): Evidence for a specific microwave radiation effect on the green fluorescent protein
• Weissenborn R et al. (2005): Non-thermal microwave effects on protein dynamics? An X-ray diffraction study on tetragonal lysozyme crystals
• Mancinelli F et al. (2004): Non-thermal effects of electromagnetic fields at mobile phone frequency on the refolding of an intracellular protein: myoglobin
• de Pomerai DI et al. (2003): Microwave radiation can alter protein conformation without bulk heating
• Bismuto E et al. (2003): Are the conformational dynamics and the ligand binding properties of myoglobin affected by exposure to microwave radiation?
• Bohr H et al. (2000): Microwave-enhanced folding and denaturation of globular proteins