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A comparison of the dielectric behaviour of human haemoglobin SC with SS and AA in solution
A A Laogun1, E H Agba, N O Ajayi
1International Centre for Theoretical Physics, Trieste, Italy.
Haemoglobin (Hb) SC is one of the most prevalent sickle-cell disorders. Patients with Hb SC are known to inherit a befa(S)-globin gene from one parent and a beta(C)-globin gene from the other. The radiofrequency dielectric properties of heterozygous Hb SC have been investigated and compared with those of homozygous Hb SS and AA in solution. The relative permittivity, epsilon', the dielectric loss factor, epsilon", and the energy dissipation factor, tan delta, of the different haemoglobin samples have been measured in the frequency range 0.1-50.0 MHz using a TF1245 Marconi Q-meter working in conjunction with a TF1246 oscillator at a room temperature of 26.0 +/- 0.5 degrees C. The Hb SC samples were found to exhibit dielectric dispersions distinctly different from those of Hb SS and AA. The dielectric data were fitted to the Cole-Cole structural equation and the fitted parameters are presented. The results are discussed on the basis of the molecular structure and polymerization characteristics of the haemoglobins in solution.
Haemoglobin (Hb) SC is one of the most prevalent sickle-cell disorders. Patients with Hb SC are known to inherit a befa(S)-globin gene from one parent and a beta(C)-globin gene from the other. The radiofrequency dielectric properties of heterozygous Hb SC have been investigated and compared with those of homozygous Hb SS and AA in solution. The relative permittivity, epsilon', the dielectric loss factor, epsilon", and the energy dissipation factor, tan delta, of the different haemoglobin samples have been measured in the frequency range 0.1-50.0 MHz using a TF1245 Marconi Q-meter working in conjunction with a TF1246 oscillator at a room temperature of 26.0 +/- 0.5 degrees C. The Hb SC samples were found to exhibit dielectric dispersions distinctly different from those of Hb SS and AA. The dielectric data were fitted to the Cole-Cole structural equation and the fitted parameters are presented. The results are discussed on the basis of the molecular structure and polymerization characteristics of the haemoglobins in solution.