Haemoglobin site-specifically modified with ferulic acid to suppress the autoxidation

References

• Winslow RM. Progress on blood substitutes. Nat Med. 1997;3:474.
   PubMed Web of Science ®Google Scholar
• Chang TMS. Blood substitutes: principles, methods, products and clinical trials. Switzerland: S. Karger AG; 1997.
   Google Scholar
• Tsuchida E, editor. 1998. Blood substitutes: present and Future Perspectives. Amsterdam: Elsevier Science.
   Google Scholar
• Reiss JG. Oxygen carriers (“blood substitutes”)-raison d’etre, chemistry, and some physiology. Chem Rev. 2001;101:2797–2920.
   PubMed Web of Science ®Google Scholar
• D’Agnillo F, Alayash AI. Redox cycling of diaspirincross-liked hemoglobin induced G2/M arrest and apoptosis in cultured endothelial cells. Blood. 2001;98:3315–3323.
   PubMed Web of Science ®Google Scholar
• Conover CD, Lejeune L, Shum KL, et al. Physiological effect of polyethylene glycol conjugation on stroma-free bovine hemoglobin in the conscious dog after partial exchange transfusion. Artif Organs. 1997;21:369–378.
   PubMed Web of Science ®Google Scholar
• Hess JR. Blood substitutes for surgery and trauma: efficacy and toxicity issues. BioDrugs. 1999;12:81–91.
   PubMed Web of Science ®Google Scholar
• Takeoka S, Teramura Y, Atoji T, et al. Effect of Hb-encapsulation with vesicles on H2O2 reaction and lipid peroxidation. Bioconjug Chem. 2002;13:1302–1308.
   PubMed Web of Science ®Google Scholar
• Teramura Y, Kanazawa H, Sakai H, et al. Prolonged oxygen-carrying ability of hemoglobin vesicles by coencapsulation of catalase in vivo. Bioconjug Chem. 2003;14:1171–1176.
   PubMed Web of Science ®Google Scholar
• Lee R, Neya K, Svizzero TA, et al. Limitations of the efficacy of hemoglobin-based oxygen-carrying solutions. J Appl Physiol 1995;78:236–242.
   Web of Science ®Google Scholar
• Faivre B, Menu B, Labrude P, et al. Hemoglobin autooxidation/oxidation mechanisms and methemoglobin prevention or reduction processes in the bloodstream. Literature review and outline of autooxidation reaction. Artif Cells Blood Subs Immob Biotech. 1998;26:17–26.
   PubMed Web of Science ®Google Scholar
• Linberg R, Conover CD, Shum KL, et al. Hemoglobin based oxygen carriers: how much methemoglobin is too much? Artif Cells Blood Substit Immobil Biotechnol. 1998;26:133–148.
   PubMed Web of Science ®Google Scholar
• Everse J, Hsia N. The Toxicities of Native and Modified Hemoglobins. Free Radic Biol Med. 1997;22:1075–1099.
   PubMed Web of Science ®Google Scholar
• Nagababu E, Rifkind JM. Reaction of Hydrogen Peroxide with ferrylhemoglobin: superoxide production and heme degradation. Biochemistry. 2000;39:12503–12511.
   PubMed Web of Science ®Google Scholar
• Cadenas E. Biochemistry of oxygen toxicity. Annu Rev Biochem. 1989;58:79–110.
   PubMed Web of Science ®Google Scholar
• Shikama K. A controversy on the mechanism of autoxidation of oxymyoglobin and oxyhaemoglobin: oxidation, dissociation, or displacement? Biochem J. 1984;223:279–280.
   PubMed Web of Science ®Google Scholar
• Tomoda A, Yoneyama T, Tsuji A. Changes in intermediate haemoglobins during autoxidation of haemoglobin. Biochem J. 1981;195:485–492.
   PubMed Web of Science ®Google Scholar
• Naito Y, Fukutomi I, Masada Y, et al. Virus removal from hemoglobin solution using Planova membrane. Artif Organs. 2002;5:141–145.
   Google Scholar
• Walter SV, Chang TMS. Chronotropic effects of in vitro perfusion with albumin, stroma-free hemoglobin, and polyhemoglobin solutions. Biomater Artif Cells Artif Organs. 1990;18:283–298.
   PubMed Web of Science ®Google Scholar
• Wang MY, Yu YT, Chang TMS. New method for preparing more stable microcapsules for the entrapment of genetically engineered cells. Artif Cells Blood Subs Immob Biotech. 2005;33:257–269.
   PubMed Web of Science ®Google Scholar
• Gu J, Chang TMS. Extraction of erythrocyte enzymes for the preparation of polyhemoglobin-catalase-superoxide dismutase. Artif Cells Blood Subs and Biotech. 2009;37:69–77.
   PubMed Web of Science ®Google Scholar
• D’Agnillo F, Chang TMS. Polyhemoglobin-superoxide dismutase-catalase as a blood substitute with antioxidant properties. Nat Biotech. 1998;16:667–671.
   PubMed Web of Science ®Google Scholar
• Alagic A, Koprianiuk A, Kluger R. Hemoglobin-superoxide dismutase-chemical linkages that create a dual-function protein. J Am Chem Soc. 2005;127:8036–8043.
   PubMed Web of Science ®Google Scholar
• Mathew S, Abraham T. Ferulic acid: an antioxidant found naturally in plant cell walls and feruloyl esterases involved in its release and their applications. Crit Rev Biotechnol. 2004;24:59–83.
   PubMed Web of Science ®Google Scholar
• Walder RY, Andracki ME, Walder JA. Preparation of intramolecularly cross-linked hemoglobins. Meth Enzymol. 1994;231:274–280.
   PubMed Web of Science ®Google Scholar
• Abugo OO, Rifkind JM. Oxidation of hemoglobin and the enhancement produced by nitroblue tetrazolium. J Biol Chem. 1994;269:24845–24853.
   PubMed Web of Science ®Google Scholar
• Alayash AI, Summers AG, Wood F, et al. Effects of glutaraldehyde polymerization on oxygen transport and redox properties of bovine hemoglobin. Arch Biochem Biophys. 2001;391:225–234.
   PubMed Web of Science ®Google Scholar
• Nicholson SK, Tucker GA, Brameld JM. Effects of dietary polyphenols on gene expression in human vascular endothelial cells. Proc Nutr Soc. 2008;67:42–47.
   PubMed Web of Science ®Google Scholar