ENG  Vol.4 No.10 , October 2012
Mathematical Modeling of Hemoglobin Release under Hypotonic Conditions
Abstract
Mathematical model is developed to estimate hemoglobin release under hypotonic conditions at microscopic level. The phenomenon of hemoglobin (Hb) release depends on: 1) the dynamics of repeated opening of hemolytic holes and 2) the radial fluctuations of lipid membrane. Both processes are sensitive to the rate of ionic strength decrease within the surrounding medium. Influence of the rate of ionic strength decrease on hemoglobin release is quantified by the model parameters: 1) the specific decrease of erythrocyte radius and 2) the specific decrease of hole radius during single opening time period of hemolytic hole. The prediction of released amount of Hb influenced by the conductive mechanism is equal to 2.9 %. The prediction of total released amount of Hb influenced by the conductive and convective mechanisms is approximately equal to 4 % of the initial amount of Hb within erythrocyte.

Cite this paper
I. Pajic-Lijakovic, B. Bugarski and M. Plavsic, "Mathematical Modeling of Hemoglobin Release under Hypotonic Conditions," Engineering, Vol. 4 No. 10, 2012, pp. 176-179. doi: 10.4236/eng.2012.410B046.
References

[1]   S.M. Christensen, F. Medina, R.W. Winslow, S.M Snell, A. Zegna, M.A. Marini, “Preparation of human hemoglobin Ao for possible use as a blood substitute” J. Biochem. Biophys. Methods 1988;17, pp. 143-54, 1988.

[2]   B. Bugarski, N. Dovezenski, Hemofarm Koncern. Verfahren zur Herstellung von Hemoglobin, Deutsches Patentamt DE 19707508, 2000.

[3]   M.R. Leiber, T.L. Steck, “A description of the holes in human erythrocyte membrane ghosts”, J. Biol. Chem. 257, pp.11651-11659, 1982.

[4]   Y. Sato, H. Yamakose, Y. Suzuki, “Participation of Band 3 Protein in Hypotonic Hemolysis of Hyman Erythrocytes”, Biol. Pharmac. Bul. 16(2), pp. 188-194, 1993.

[5]   A. Pribush, D. Meyerstein, N. Meyerstein, “Kinetic of erythrocyte swelling and membrane hole formation in hypotonic media”, Biochem. Biophys. Acta 1558, pp. 119-132, 2002.

[6]   I. Pajic-Lijakovic, V. Ilic, B. Bugarski, M. Plavsic,“The rearrangement of erythrocyte band 3 molecules and reversible osmotic holes formation under hypotonic conditions”, Europ. Biophys. J. 39(5), pp. 789-797, 2010.

[7]   M. Delano, “Simple physical constraints in hemolysis”, J. Theor. Biol. 175, pp. 517-524, 1995.

[8]   A.M.M. Zade-Oppen, “Repetitive cell 'jump' during hypotonic lyses of erythrocytes observed with simple flow chamber”, J. Microsc. 192, pp. 54-62, 1998.

[9]   G.B. Nash, H.J. Meiselman, “Red Cell and Ghost Viscoelasticity, Effects of Hemoglobin Concentration and In Vivo Aging”, Biophys. J. 43, pp. 63-73, 1983.

[10]   R. Shuklar, M. Balakrishnan, G.P. Agarwal, “Bovine serum albumin-hemoglobin fractionation: significance of ultra filtration system and feed solution characteristics”, Bioseparation 9, pp. 7-19, 2000.

[11]   V. Riveros-Moreno, J.B. Wittenberg, “The Self-Diffusion Coefficients of Myoglobin and Hemoglobin in Concentrated Solutions”, J. Biol. Chem. 247(3), pp. 895-901, 1972.

[12]   W. Doster, S. Longeville, “Microscopic Diffusion and Hydrodynamics of Hemoglobin in Red Blood Cells”, Biophys. J. 93, pp. 1360-1368, 2007.

[13]   A.M. Gennario, A. Luquita, M. Rasia, “Comparison between Internal Microviscosity of Low-Density Erythrocytes and the Microviscosity of Hemoglobin Solutions: An Electron Paramagnetic Resonance Study”, Biophys. J. 71, pp. 389-393, 1996.

[14]   D.P. Ross, A.P. Minton, “Analysis of non-ideal behavior in concentrated hemoglobin solution”, J. Molec. Biol. 112, pp. 437-452, 1977.

 
 
Top