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Kinetics of Denaturation of Human and Chicken Hemoglobins in the Presence of Co-solvents

  • Ajloo, Davood (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Moosavi-Movahedi, Ali A. (Institute of Biochemistry and Biophysics, University of Tehran)
  • Received : 2002.12.02
  • Accepted : 2003.02.25
  • Published : 2003.07.31

Abstract

The stability of four hemoglobins (Hb) in dimer forms (low concentration) were investigated by the kinetics of denaturation. The rate constants of denaturation were obtained by variation of 280 nm absorption versus time in 10 mM Tris-HCl, 10 mM EDTA, pH 8.0 at $45^{\circ}C$ in the absence and presence of 0.5 M ethanol, dimethyl sulfoxide (DMSO), formamide, and glycerol. The results show the trend of rate constants in different co-solvents in the following order: chicken hemolysate < human hemolysate and chicken Hb D < chicken Hb A. The buried surface area was calculated for Hb samples in the absence of cosolvents. Accordingly, the trend points out that: chicken Hb D > chicken Hb A > human Hb A. These results suggest that both chicken hemolysate and chicken Hb D are relatively more stable than human and chicken Hb A, respectively. However, the denaturation rate constants of Hb in different co-solvents have designated the following order: ethanol > DMSO > formamide > glycerol. As a matter of fact, this phenomenon is an indication of an increase in the denaturation capacity (DC) and hydrophobicity, and a decrease in the surface tension of the solution in the preceding co-solvents.

Keywords

References

  1. Abraham, M. H., Choda, H. S., Whiting, G. S. and Mitchell, R.C. (1994) Hydrogen bonding: An analysis of water-octanol and water-alkane partitioning and the ${\Delta}log$ P parameters of Seiler. J. Pharm. Sci. 83, 1085-1100. https://doi.org/10.1002/jps.2600830806
  2. Ajloo, D., Moosavi-Movahedi, A. A., Hakimelahi, G. H., Saboury,A. A. and Gharibi, H. (2002a) The effect of dodecyl trimethylammonium bromide on the formation of methemoglobins and hemichrome. Colloids and Surfaces B: Biointerfaces 26, 185-196. https://doi.org/10.1016/S0927-7765(02)00003-6
  3. Ajloo, D., Moosavi-Movahedi, A. A., Sadeghi, M. and Gharibi, H.(2002b) Comparative structural and functional studies of avian and mammalian hemoglobins. Acta Biochim. Pol. 49, 459-470.
  4. Baldwin, R. L. (1996) How Hofmeister ion interactions affect protein stability. Biophys. J. 71, 2056-5063. https://doi.org/10.1016/S0006-3495(96)79404-3
  5. Benson, S. W. (1960) Infinite sequence of first-order reactions; in The Foundations of Chemical Kinetics, pp. 36-42, McGraw-Hill, New York, USA.
  6. Bonger, P., Csutora, P., Cameron, I. L., Wheatley, D. N. andMiseta, A. (1998) Augmented water binding and low cellular water in erythrocytes of camel and camelids. Biophys. J. 75, 3085-3091. https://doi.org/10.1016/S0006-3495(98)77749-5
  7. Bordbar, A. K. and Moosavi-Movahedi, A. A. (1996) Binding data analysis of the interaction of bovine hemoglobin with dodecyltrimethylammonium bromide Bull. Chem. Soc. Jpn. 69, 2231-2234. https://doi.org/10.1246/bcsj.69.2231
  8. Bordbar, A. K., Nasehzadeh, A., Ajloo, D., Omydiyan, K.,Naghibi, H., Mehrabi, M., Khajehpour, H., Rezaie-Tavirani M.and Moosavi-Movahedi, A. A. (2002) Thermodynamics elucidation of binding isotherms for hemoglobin & globin of human and bovine upon interaction with dodecyltrimethylammonium bromide Bull. Korean Chem. Soc. 23, 1073-1077. https://doi.org/10.5012/bkcs.2002.23.8.1073
  9. Cobb, J. A., Manning, D., Kolatkar, P. R., Cox, D. J. and Riggs, A. F. (1992) Deoxygenation-linked association of tetrameric component of chicken hemoglobin. J. Biol. Chem. 267, 1183-1189.
  10. Colombo, M. F., Rau, D. C. and Parsegian, V. A. (1992) Protein solvation in allosteric regulation a water effect on hemoglobin. Science 256, 655-659. https://doi.org/10.1126/science.1585178
  11. Dayer, M. R., Moosavi-Movahedi, A. A., Norouzi, P., Ghourchian,H. and Safarian, S. (2002) Inhibition of human hemoglobin autoxidation by sodium n-dodecyl sulphate. J. Biochem. Mol. Biol. 35, 364-370. https://doi.org/10.5483/BMBRep.2002.35.4.364
  12. Dean, J. A. (1992) Lange’s Handbook of Chemistry, 14th ed., McGraw-Hill, New York, USA.
  13. Guidotti, G. (1967) Studies on the chemistry of hemoglobin. II. The effect of salts on the dissociation of hemoglobin into subunits. J. Biol. Chem. 242, 3685-3693.
  14. Herskovits, T. T., Behrens, C. F. Siuta, P. B. and Pandolfelli, E. R.(1977) Solvent denaturation of globular proteins; unfolding by monoalkyl and dialkyl- substituted formamides and ureas. Biochim. Biophys. Acta 490, 192-199. https://doi.org/10.1016/0005-2795(77)90119-2
  15. Khmelnitsky, Y. L., Mozhaev, V. V., Belova, A. B., Sergeeva M. V. and Martinek, K. (1991) Denaturation capacity: a new quantitative criterion for selection of organic solvents as reaction media in biocatalysis. Eur. J. Biochem. 198, 31-41. https://doi.org/10.1111/j.1432-1033.1991.tb15983.x
  16. Kinderlerer, J., Lehmann, H. and Tipton, K. F. (1971) The thermal denaturation of human oxyhemoglobins A, $A_2$, C and S. Biochem. J. 135, 805-814.
  17. Knapp, J. E., Oliveira, M. A., Xie, Q., Ernst, S. R. and Riggs, A.F. (1999) The structural and functional analysis of the hemoglobin D component from chicken. J. Biol. Chem. 274, 6411-6420. https://doi.org/10.1074/jbc.274.10.6411
  18. Kumar, S., Tsai, C. and Nussinov, R. (2000) Factor enhancing protein thermostability. Protein Eng. 13, 179-191. https://doi.org/10.1093/protein/13.3.179
  19. Liu, C., Bo, A., Cheng, G., Lin, X. and Dong, S. (1998)Characterization of structural and functional changes of hemoglobin in dimethyl sulfoxide by spectroscopic techniques. Biochim. Biophys. Acta 1385, 53-60. https://doi.org/10.1016/S0167-4838(98)00044-2
  20. Militello, V., Vitrano, E. and Cupane, E. (1991) The effect of organic co-solvents on the oxygen affinity of fetal hemoglobin relevance of protein-solvent interaction to functional properties. Biophys. Chem. 39, 161-169. https://doi.org/10.1016/0301-4622(91)85018-L
  21. Perutz, M. F. and Raidt, H. (1975) Stereochemical basis of heat stability in bacterial ferredoxins and in hemoglobin A2. Nature 255, 256-259. https://doi.org/10.1038/255256a0
  22. Rosell, C. M., Vaidya, A. M. and Halling, P. J. (1995) Prediction of denatiration tendency of organic solvents in mixtures with water by measurement of naphthalene solubility. Biochim. Biophys. Acta 1252, 158-164. https://doi.org/10.1016/0167-4838(95)00128-H
  23. Shrake, A. and Rupley, J. A. (1973) Environment and exposure to solvent of protein atoms, lysozyme and insulin. J. Mol. Biol. 79, 351-371. https://doi.org/10.1016/0022-2836(73)90011-9
  24. Williams, R. C. and Tsay, K. Y. (1973) A convenient chromatographic method for the preparation of human hemoglobin. Anal. Biochem. 54, 137-145. https://doi.org/10.1016/0003-2697(73)90256-X

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