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생화학분자생물학회 (Korean Society for Biochemistry and Molecular Biology)
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Inhibition of Human Hemoglobin Autoxidaiton by Sodium n-Dodecyl Sulphate

  • 발행 : 2002.07.31
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초록

The effect of sodium n-dodecyl sulphate (SDS) on hemoglobin autoxidation was studied in the presence of a 100mM phosphate buffer (pH 7.0) by different methods. These included spectorphotometry, fluorescence technique, cyclic voltametry, differential scanning calorimetry, and densitometry. Spectroscopic studies showed that SDS concentrations up to 1 mM increased deoxy-, decreases oxy-, and had no significant effect on the met- conformation of hemoglobin. Therefore, a SDS concentration up to 1 mM increased the deoxy form of hemoglobin as the folded, compact state and decreases the oxy conformation. The turbidity measurements and differential scanning calorimetry techniques indicated a more stable conformation for hemoglobin in the presence of SDS up to 1mM. Electrochemical studies also confirmed a more difficult oxidation under these conditions. The induction of the deoxy form in the presence of SDS was confirmed by densitometry techniques. The compact structure of deoxyhemoglobin blocks the formation of met-conformation in low SDS concentrations.

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참고문헌

  1. Antonini, E. and Brunori, M. (1971) Hemoglobin and myoglobin in their reaction with ligands, North-Holland Publishing Co., Amsterdam.
  2. Arakawa, T. and Timasheff, S. N. (1982) Stabilization of protein structure by sugars. Biochemistry 21, 6534-6544.
  3. Baldwin, J. N. and Ye, R. P. (1988) Catalytic reduction of myoglobin and hemoglobin at chemically modified electrodes containing methylene blue. Anal. Chem. 60, 2263-2268. https://doi.org/10.1021/ac00171a021
  4. Banerjee, R. and Cassoly, R. (1969) Preparation and properties of the isolated alpha and beta chains of human hemoglobin in the ferri state. Investigation of oxidation-reduction equilibria. J Mol. Biol. 42, 337-349. https://doi.org/10.1016/0022-2836(69)90047-3
  5. Benesch, R. E. Benesch, R. and Yung, S. (1973) Equations for the spectrophotometric analysis of hemoglobin mixtures. Anal. Biochem. 55, 245-248. https://doi.org/10.1016/0003-2697(73)90309-6
  6. Berman, M. Benesch, R. and Benesch, R. E. (1971) The removal of organic phosphates from hemoglobin. Arch. Biochem. Biophys. 145, 236-239. https://doi.org/10.1016/0003-9861(71)90031-2
  7. Bonaventura, C. Tesh, S. Faulkner, K. M. Kraiter, D. and Crumbliss, A. L. (1998) Conformational fluctuations in deoxy hemoglobin revealed as a major contributor to anionic modulation of function through studies of the oxygenation and oxidation of hemoglobin $A_{0}$ and Hemoglobin Deer Lodge b2(NA2) His $\rightarrow$ Arg). Biochemistry 35, 496-506.
  8. Bordbar, A. K. Moosavi-MovalIedi, A. A. and Saboury, A. A. (1996) Comparative thermodynamical stability of bovine and pigeon hemoglobin by interaction with sodium n-dodecyl sulphate. Thermochimica Acta 287, 343-349. https://doi.org/10.1016/S0040-6031(96)03000-6
  9. Boyiri, T. Safo, M. K. Danso-DangualI, R. E. Kister, J. Poyart, C. and AbralIam, D. J. (1995) Bisaldehyde allosteric effectors as molecular ratchets and probes. Biochemistry 34, 15021-15036. https://doi.org/10.1021/bi00046a008
  10. Brabec, V (1996) Experimental Techniques in Bioelectrochem. Vol. 3 Birkhauser Verlag, Germany.
  11. Brantley, R. E. Jr. Semerdon, S. J. Wilkinson, A. J. Singleton, E. W. and Olson, J. S. (1993) The mechanism of autoxidation of myoglobin. J. Biol. Chem. 268, 6995-7010.
  12. Bunn, H. F. and Forget, B. G. (1986) Hemoglobin: Molecular Genetic and Clinical Aspects, Saunders Company, Philadelphia, PA.
  13. Coletta, M. Ascenzi, P. Santucci, R. Bertollini, A. and Amconi, G. (1993) Interaction of inositol hexakisphosphate with liganded ferrous human hemoglobin, direct evidence for two functionally operative binding site. Biochem. Biophys. Acta 1162, 309-314. https://doi.org/10.1016/0167-4838(93)90295-3
  14. Desbois, A. and Bangerjee, R. (1975) Effects of polyvalent anion binding to hemoglobin on oxygen and oxidation-reduction equilibria and their relevance to allosteric transition. J Mol.Biol. 92, 479-493. https://doi.org/10.1016/0022-2836(75)90293-4
  15. Dickerson, L. D. Sauer-Masarwa, A. Herron, N. Fendrick, C. M. and Busch, D.H. (1993) The electron-transfer mechanism of autoxidation for hemoglobin, myoglobin, and their iron ($\Pi$) cyclidene models. J. Am. Chem. Soc. 115, 3623-3626. https://doi.org/10.1021/ja00062a028
  16. Dickinson, L. C. and Chien, J. C. (1975) Electron transfer between hemoglobin and coboglobin mediated by methylene blue. J. Am. Chem. Soc. 97, 2620-2625. https://doi.org/10.1021/ja00843a005
  17. Dong, A. Huang, P. Caughey, B. and Caughey, W. S. (1995) Infrared analysis of ligand and oxidation induced conformational changes in hemoglobins and myoglobins. Arch. Biochem. Biophys. 316, 893-898. https://doi.org/10.1006/abbi.1995.1120
  18. Fauikner, K. M. Bonaventura, C. and Crumbliss, A. L. (1995) A spectroelectrochemical method for differentiation of steric and electronic effects in hemoglobin and myoglobins. J. Biol. Chem. 270, 13404-13412.
  19. Freifelder, D. (1982) Physical Biochemistry: Applications to Biology, W. H. Freeman and Company, New York, New York.
  20. Gary, R. D. and Gibson, Q. H. (1971) The effect of inositol hexaphosphate on the kinetics of CO and $O_{2}$ binding by human hemoglobin. J. Biol. Chem. 246, 7158-7174.
  21. Geraci, S. and Sada, A. (1972) Reactivity of the 93 sulphydryls of human hemoglobin A: influence of the C-terminal residues. J. Mol. Biol. 70, 729-734. https://doi.org/10.1016/0022-2836(72)90571-2
  22. Ho, C. Eaton, W. A. Collman, J. P. Gibson, Q. H. Leigh, J. S. Jr. Margoliash, E. Moffat, K. and Scheidt, W. R. (1982) Hemoglobin and Oxygen Binding, Macmillan Press. Ltd. London.
  23. Karniyama, T. Sadahide, Y. Nogusa, Y. and Gekko, K. (1999) Polyol induced molten globule of cytochrome C: an evidence for stabilization by hydrophobic interaction. Biochim. Biophys. Acta 1434, 44-57. https://doi.org/10.1016/S0167-4838(99)00159-4
  24. Kilmartin, J. V. (1973) The interaction of inositol hexaphosphate with methaemoglobin. Biochem. J. 133,725-733. https://doi.org/10.1042/bj1330725
  25. MacDonald, V. W. and Charache, S. (1982) Comparison of the effects of lower monohydric alcohol and inositol hexaphosphate on the oxidation of hemoglobin by menadion. Biochim. Biophys. Acta 705, 48-54. https://doi.org/10.1016/0167-4838(82)90334-X
  26. Mansouri, A. and Winterhalter, K. H. (1974) Nonequivalence of chains in hemoglobin oxidation and oxygen binding, effect of organic phosphates. Biochemistry 13, 3311-3314. https://doi.org/10.1021/bi00713a021
  27. Mizukoshi, H. Itoh, M. Matsakawa, S. Mawatari, K. and Yoneyama, Y. (1982) Tryptophan fluorescence of human hemoglobin. Biochim. Biophys. Acta 700, 143-147. https://doi.org/10.1016/0167-4838(82)90090-5
  28. Moosavi-Movahedi, A. A. Rabbani, A. Goodarzi, M. and Goliaei, B. (1989) Thermodynamic studies of the interaction of sodium n-dodecyl sulphate with histone H1. Thermochimica Acta 154, 205-212. https://doi.org/10.1016/0040-6031(89)85456-5
  29. Moosavi-Movahedi, A. A. and Ghobadi, S. (1991) Thermochemical analysis of the interaction between aspergillus niger catalase and sodium n-dodecyl sulphate. Thermochimica Acta 189, 201-207. https://doi.org/10.1016/0040-6031(91)87116-E
  30. Moosavi-Movahedi, A. A. (1994) lnteraction of aspergillus niger catalase with sodium n-dodecyl sulphate. lUPAC 66, 71-75.
  31. Moosavi-Movahedi, A. A. Naderi, G. A. and Farzami, B. (1994) Denaturation behavior of calmodulin in guanidine hydrochloride, urea, sodium n-dodecyl sulphate and dodecyl trirnethylammonium bromide. Thermochimica Acta 239, 61-71.
  32. Moosavi-Movahedi, A. A. Nazari, K. and Saboury, A. A. (1997) Denaturation of horseradish peroxidase with sodium n-dodecyl sulphate and dodecyl trimethyl ammonium bromide. Colloid and Surfaces B: Biointerfaces 9, 123-130. https://doi.org/10.1016/S0927-7765(97)00016-7
  33. Nazari, K. Saboury, A. A. and Moosavi-Movahedi, A. A. (1997) Enthalpy investigation for elucidation of the transition concentration for the interaction of horseradish peroxidase with surfactants. Themochimica Acta 302, 131-135. https://doi.org/10.1016/S0040-6031(97)00211-6
  34. Riggs, A. (1981) Preparation of blood hemoglobins of vertebrates. Methods Enzymol. 76, 5-29. https://doi.org/10.1016/0076-6879(81)76111-1
  35. Safo, M. K. Moure, C. M. Bumett, J. C. Joshi, G. S. and Abraham, D. J. (2001) High-resolution crystal structure of deoxy hemoglobin complexed with a potent allosteric effector. Protein Science 10, 951-957. https://doi.org/10.1110/ps.50601
  36. Satoh, Y. and Shikama, K. (1981) Autoxidation of oxymyoglobin. A nucleophilic displacement mechanism. J. Biol. Chem. 256, 10272-10275.
  37. Schlereth, D. D. and Mantele, W. (1992) Redox-induced conformational changes in myoglobin and hemoglobin: electrochemistry and ultraviolet-visible and fourier transform infrared difference spectroscopy at surface-modified gold electrodes in an ultra-thin-Iayer spectroelectrochemical cell. Biochemistry 31, 7494-7502. https://doi.org/10.1021/bi00148a009
  38. Shikama, K. (1984) A controversy on the mechanism of autoxidation of oxymyoglobin and oxyhaemoglobin: oxidation, dissociation, or displacement? Biochem. J. 223, 279-280. https://doi.org/10.1042/bj2230279
  39. Skoog, D. A. and Leary, J. J. (1992) Principles of Instrumental Analysis, Saunders College Publishing, 4th ed. New York, New York.
  40. Stargardt, J. F. Awkridge, F. M. and Lanrum, H. L. (1978) Reversible heterogeneous reduction and oxidation of sperm whale myoglobin at a surface modified gold minigrid electrode. Anal. Chem. 50, 930-932. https://doi.org/10.1021/ac50029a026
  41. Wallace, W. J. Houtchens, R. A. Maxwell, J. C. and Caughey, W. S. (1982) Mechanism of autoxidation for hemoglobins and myoglobins. promotion of superoxide production by protons and anions. J. Biol. Chem. 257, 4966-4977.
  42. William, R. C. Jr. 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
  43. Zavodnik, I. B. Piletskaia T. P. and Stepuro, l. I. (1992) Autoxidation and oxygenation of human hemoglobin. Mol. Biol. (Mosk) 26, 321-327.

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