Derivatization of haemoglobin with periodate-generated reticulation agents: Evaluation of oxidative reactivity for potential blood substitutes

Journal of Biochemistry

Volumn 149, Issue 1, 2011, Pages 75-82

  Deac, Florina ^a   Iacob, Bianca ^a   Fischer Fodor, Eva ^b   Damian, Grigore ^a   Silaghi Dumitrescu, Radu ^a  

^a BABE BOLYAI UNIVERSITY   (Romania)

^b Cancer Institute Ion Chiricuta Cluj Napoca   (Romania)

Author keywords

Blood substitute; free radical; haemoglobin; high valent iron; oxidative stress

Indexed keywords

ADENOSINE TRIPHOSPHATE; BLOOD SUBSTITUTE; FREE RADICAL; HEMOGLOBIN; HYDROXYL GROUP; IRON; MACROGOL; PERIODATE; PEROXIDE; STARCH;

ARTICLE; CROSS LINKING; DERIVATIZATION; GEL PERMEATION CHROMATOGRAPHY; HUMAN; HUMAN CELL; OXIDATION REDUCTION REACTION; OXYGEN AFFINITY;

ADENOSINE TRIPHOSPHATE; ANIMALS; BLOOD SUBSTITUTES; CATTLE; CELLS, CULTURED; CROSS-LINKING REAGENTS; FREE RADICALS; HEMOGLOBINS; HUMANS; MOLECULAR WEIGHT; OXIDATION-REDUCTION; OXYGEN; PERIODIC ACID; POLYETHYLENE GLYCOLS; POLYMERIZATION; STARCH; UMBILICAL VEINS;

EID: 78650644431     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvq123     Document Type: Article

References (26)

1. Alayash, A.I. (2004) Oxygen therapeutics: can we tame haemoglobin? Nat. Rev. Drug Discov. 3, 152-159
2. Chang, T.M.S. (2009) Nanobiotechnology for hemoglobin based blood substitutes. Crit. Care Clinics 25, 373-382
3. Sono, M., Roach, M.P., Coulter, E.D., and Dawson, J.H. (1996) Heme-containing oxygenases. Chem. Rev. 96, 2841-2888
4. Shaik, S., Kumar, D., de Visser, S.P., Altun, A., and Thiel, W. (2005) Theoretical perspective on the structure and mechanism of cytochrome P450 enzymes. Chem. Rev. 105, 2279-2328
5. Silaghi-Dumitrescu, R., Reeder, B.J., Nicholls, P., Cooper, C.E., and Wilson, M.T. (2007) Ferryl haem protonation gates peroxidatic reactivity in globins. Biochem. J. 403, 391-395
6. Reeder, B.J., Grey, M., Silaghi-Dumitrescu, R.L., Svistunenko, D.A., Bulow, L., Cooper, C.E., and Wilson, M.T. (2008) Tyrosine residues as redox cofactors in human hemoglobin: implications for engineering nontoxic blood substitutes. J. Biol. Chem. 283, 30780-30787
7. Reeder, B.J., Svistunenko, D.A., Cooper, C.E., and Wilson, M.T. (2004) The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology. Antioxidant Redox Signaling 6, 954-966
8. Olson, J.S., Foley, E.W., Rogge, C, Tsai, A.L., Doyle, M.P., and Lemon, D.D. (2004) NO scavenging and the hypertensive effect of hemoglobin-based blood substitutes. Free Radic. Biol. Med. 36, 685-697
9. Chen, J.Y., Scerbo, M., and Kramer, G. (2009) A review of blood substitutes: examining the history, clinical trial results, and ethics of hemoglobin-based oxygen carriers. Clinics 64, 803-813
10. Harris, D.R. and Palmer, A.F. (2008) Modern cross-linking strategies for synthesizing acellular hemoglobin-based oxygen carriers. Biotechnol. Prog. 24, 1215-1225
11. Simoni, J., Simoni, G., Newman, G., and Feola, M. (1996) An improved blood substitute. In vivo evaluation of its hemodynamic effects. Asaio J. 42, M773-M782
12. Riess, J.G. (2001) Oxygen carriers (''Blood Substitutes'') sRaison d'Etre, chemistry, and some physiology. Chem. Rev. 101, 2797-2919
13. Eike, J.H. and Palmer, A.F. (2004) Oxidized mono-, di-, tri-, and polysaccharides as potential hemoglobin cross-linking reagents for the synthesis of high oxygen affinity artificial blood substitutes. Biotechnol. Prog. 20, 953-962
14. Antonini, E. and Brunori, M. (1971) Hemoglobin and Myoglobin in their Reaction with Ligands, North-Holland, Amsterdam, Holland
15. Denizot, F. and Lang, R. (1986) Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability. J. Immunol. Methods 89, 271-277
16. Furukawa, T., Kubota, T., Suto, A., Takahara, T., Yamaguchi, H., Takeuchi, T., Kase, S., Kodaira, S., Ishibiki, K, and Kitajima, M. (1991) Clinical usefulness of chemosensitivity testing using the MTT assay. J. Surg. Oncol. 48, 188-193
17. Cooper, C.E., Silaghi-Dumitrescu, R., Rukengwa, M., Alayash, A.I., and Buehler, P.W. (2008) Peroxidase activity of hemoglobin towards ascorbate and urate: a synergistic protective strategy against toxicity of hemoglobin-based oxygen carriers (HBOC). Biochim. Biophys. Acta 1784, 1415-1420
18. Deac, F.V., Todea, A., Bolfa, A.M., Podea, P., Petrar, P., and Silaghi-Dumitrescu, R. (2009) Ascorbate binding to globins. Rom. J. Biochem. 46, 115-121
19. Eike, J.H. and Palmer, A.F. (2004) Effect of NaBH4 concentration and reaction time on physical properties of glutaraldehyde-polymerized hemoglobin. Biotechnol. Prog. 20, 946-952
20. + on the oxygen binding properties of glutaraldehyde-polymerized bovine hemoglobin-based blood substitutes. Biotechnol. Prog. 20, 1543-1549
21. Eike, J.H. and Palmer, A.F. (2004) Effect of glutaralde-hyde concentration on the physical properties of polymerized hemoglobin-based oxygen carriers. Biotechnol. Prog. 20, 1225-1232
22. Deac, F., Todea, A., and Silaghi-Dumitrescu, R. (2009) Glutaraldehyde derivatization of hemoglobin: a potential blood substitute. (Silaghi-Dumrescu, R. and Garban, G., eds.), pp. 165-173, Cluj University Press, Cluj-Napoca, Romania
23. Svistunenko, D.A. (2005) Reaction of haem containing proteins and enzymes with hydroperoxides: The radical view. Biochim. Biophys. Acta 1707, 127-155
24. Buehler, P.W., Vallelian, F., Mikolajczyk, M.G., Schoedon, G., Schweizer, T., Alayash, A.I., and Schaer, D.J. (2008) Structural stabilization in tetrameric or polymeric hemoglobin determines its interaction with endogenous antioxidant scavenger pathways. Antioxid. Redox Signal. 10, 1449-1462
25. Ortegon, D.P., Davis, M.R., Dixon, P.S., Smith, D.L., Josephs, J.D., Mueller, D.L., Jenkins, D.H., and Kerby, J.D. (2002) The polymerized bovine hemoglobin-based oxygen-carrying solution (HBOC-201) is not toxic to neural cells in culture. J. Trauma 53, 1068-1072
26. Sullivan, J.P. and Palmer, A.F. (2006) Targeted oxygen delivery within hepatic hollow fiber bioreactors via supplementation of hemoglobin-based oxygen carriers. Biotechnol. Prog. 22, 1374-1387