Effects of a static magnetic field on haemoglobin structure and function. 1995

M M Atef, and M S Abd el-Baset, and A el-Kareem, and S Aida, and M A Fadel
Biochemistry Department, National Research Center, Cairo, Egypt.

The exposure of mice to static magnetic fields (MF) of different strengths (1000-4000 G) for 10 min was studied. The effects of these magnetic fields on the function of haemoglobin (Hb), and its conformational stability, auto-oxidation kinetics, bioenergetics and viscosity, and those of different Hb derivatives were investigated. The fractions and concentrations of the inactive Hb pigments (such as methaemoglobin, carboxyhaemoglobin and sulfohaemoglobin) and the active Hb (in the HbO2 form) were determined using a newly developed multi-component spectrophotometric method. The direct effect of magnetic fields of relatively high strengths (3500 and 4000 G) led to different Hb conformations, accompanied by changes in intermolecular interactions represented by the slope of the eta sp/C = F(C) lines and Huggins' constant K', while no measurable change in the intrinsic viscosity [eta] of Hb was observed. These results indicate a lack of changes in the dimensions and shape of the Hb molecule. Study of the kinetics of oxyhaemoglobin auto-oxidation revealed decreases in the auto-oxidation reaction rate of 2-5.9% and 10-17%, under the effect of static MFs of strengths 1000-2500 G and 3500-4000 G, respectively.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008280 Magnetics The study of MAGNETIC PHENOMENA. Magnetic
D008297 Male Males
D008706 Methemoglobin Ferrihemoglobin
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010108 Oxyhemoglobins A compound formed by the combination of hemoglobin and oxygen. It is a complex in which the oxygen is bound directly to the iron without causing a change from the ferrous to the ferric state. Oxycobalt Hemoglobin,Oxycobalthemoglobin,Oxyhemoglobin,Hemoglobin, Oxycobalt
D002263 Carboxyhemoglobin Carbomonoxyhemoglobin,Carbonmonoxyhemoglobin,Carbonylhemoglobin,Carboxyhemoglobin A,Carboxyhemoglobin C
D006454 Hemoglobins The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements. Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013057 Spectrum Analysis The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) Spectroscopy,Analysis, Spectrum,Spectrometry

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