Effect of different magnetic fields on hemoglobin

ABSTRACT

The effect of static magnetic fields from south and/or north poles [1000 Gauss], on the absorption spectrum, hemoglobin pattern, the thermodynamic parameters and the hemoglobin active sites were studied. The same magnetic field effects were carried out on hemoglobin of different ligands. Subjecting, or facing the samples to the south pole of the permanent magnet leads to the elevation of globin-heme and heme-heme interactions concomitant with a drop in the amount of methemoglobin and carboxyhemoglobin. Moreover, when this same pole faces carboxyhemoglobin a cleavage to hemoglobin and free carbon monoxide was detected. These parameters were less pronounced on applying both the north and south poles around the sample. Facing the sample to north pole of the magnet reversed the effect. In this case the entropy and enthalpy were increased. Moreover, the salt bridge which fixed the carbon terminals of the Hb submits was affected leading to partial dissociation to dimer and monomer