Physicochemical properties and oxygen affinity of glutaraldehyde polymerized crocodile hemoglobin: the new alternative hemoglobin source for hemoglobin-based oxygen carriers

References

• Bettati S, Viappiani C, Mozzarelli A. Hemoglobin, an “evergreen red protein”. Biochim Biophys Acta. 2009;1794:1317–1324.
   PubMed Web of Science ®Google Scholar
• Mollan TL, Alayash AB. Redox reactions of hemoglobin: mechanisms of toxicity and control. Antioxid Redox Signal. 2013;18:2251–2253.
   PubMed Web of Science ®Google Scholar
• Weiskopf RB. Hemoglobin-based oxygen carriers: disclosed history and the way ahead: the relativity of safety. Anesth Analg. 2014;119:758–760.
   PubMed Web of Science ®Google Scholar
• Buehler PW, D′Agnillo F, Schaer DJ. Hemoglobin-based oxygen carriers: from mechanisms of toxicity and clearance to rational drug design. Trends Mol Med. 2010;16:447–457.
   PubMed Web of Science ®Google Scholar
• Frietsch T, Lenz C, Waschke KF. Artificial oxygen carriers. Eur J Anaesthesiol. 1998;15:571–584.
   PubMed Web of Science ®Google Scholar
• Hess JR. An update on solutions for red cell storage. Vox Sang. 2006;91:13–19.
   PubMed Web of Science ®Google Scholar
• Macdonald S. Red cell 2,3-diphosphoglycerate and oxygen affinity. Anaesthesia. 1977;32:544–553.
   PubMed Web of Science ®Google Scholar
• Harris DR, Palmer AF. Novel strategies for transporting cellular hemoglobin-based oxygen carriers in the systemic circulation. Transfus Alternat Transfus Med. 2007;9:237–245.
   Google Scholar
• Booth C, Allard S. Blood transfusion. Medicine. 2017;45:244–250.
   Google Scholar
• Fronticelli C, Sato T, Orth C, et al. Bovine hemoglobin as a potential source of hemoglobin-based oxygen carriers: crosslinking with bis(2,3-dibromosalycyi)fumarate. Biochim Biophys Acta. 1986;874:76–81.
   PubMed Web of Science ®Google Scholar
• Komiyama NH, Miyazaki G, Tame J, et al. Transplanting a unique allosteric effect from crocodile into human haemoglobin. Nature. 1995;373:244–246.
   PubMed Web of Science ®Google Scholar
• Wang Q, Sun L, Ji S, et al. Reversible protection of Cys-93(β) by PEG alters the structural and functional properties of the PEGylated hemoglobin. Biochim Biophys Acta. 2014;1844:1201–1207.
   PubMed Web of Science ®Google Scholar
• Webster KD, Dahhan D, Otto AM, et al. Inside-out PEGylation of bovine β-cross-linked hemoglobin. Artif Organs. 2017;41:351–358.
   PubMed Web of Science ®Google Scholar
• Jandaruang J, Siritapetawee J, Songsiriritthigul C, et al. Purification, characterization, and crystallization of Crocodylus siamensis. Protein J. 2014;33:377–385.
   PubMed Web of Science ®Google Scholar
• Eike JH, Palmer AF. Effect of Cl- and H+ on the oxygen binding properties of glutaraldehyde-polymerized bovine hemoglobin-based blood substitutes. Biotechnol Prog. 2004;20:1543–1549.
   PubMed Web of Science ®Google Scholar
• Yu Z, Friso G, Miranda JJ, et al. Structural characterization of human hemoglobin crosslinked by bis(3,5-dibromosalicyl) fumarate using mass spectrometric techniques. Protein Sci. 2008;6:2568–2577.
   Google Scholar
• Modery-Pawlowski CL, Tian LL, Pan V, et al. Synthetic approaches to RBC mimicry and oxygen carrier systems. Biomacromolecules. 2013;14:939–948.
   PubMed Web of Science ®Google Scholar
• McCarthy MR, Vandegriff KD, Winslow RM. The role of facilitated diffusion in oxygen transport by cell-free hemoglobins: implications for the design of hemoglobin-based oxygen carriers. Biophys Chem. 2001;92:103–117.
   PubMed Web of Science ®Google Scholar
• Winslow RM. Current status of blood substitute research: towards a new paradigm. J Intern Med. 2003;253:508–517.
   PubMed Web of Science ®Google Scholar
• Bunn HF, Esham WT, Bull RW. The renal handling of hemoglobin. I. Glomerular filtration. J Exp Med. 1969;129:909–923.
   PubMed Web of Science ®Google Scholar
• Levy JH, Goodnough LT, Greilich PE, et al. Polymerized bovine hemoglobin solution as a replacement for allogeneic red blood cell transfusion after cardiac surgery: results of a randomized, double-blind trial. J Thorac Cardiovasc Surg. 2002;124:35–42.
   PubMed Web of Science ®Google Scholar
• Silverman TA, Weiskopf RB. Hemoglobin-based oxygen carriers: current status and future directions. Anesthesiology. 2009;111:946–963.
   PubMed Web of Science ®Google Scholar
• Grigg GC, Wells RMG, Beard LA. Allosteric control of oxygen binding by haemoglobin during embryonic development in the crocodile Crocodylus porosus: the role of red cell organic phosphate and carbon dioxide. J Exp Biol. 1993;175:15–32.
   Web of Science ®Google Scholar
• Pata S, Yaraksa N, Daduang S, et al. Characterization of the novel antibacterial peptide Leucrocin from crocodile (Crocodylus siamensis) white blood cell extracts. Dev Comp Immunol. 2011;53:545–553.
   Web of Science ®Google Scholar
• Jandaruang J, Siritapetawee J, Thumanu K, et al. The effects of temperature and pH on secondary structure and antioxidant activity of Crocodylus siamensis hemoglobin. Protein J. 2012;31:43–50.
   PubMed Web of Science ®Google Scholar
• Dimino ML, Palmer AF. Purification of bovine hemoglobin via fast performance liquid chromatography. J Chromatogr B Analyt Technol Biomed Life Sci. 2007;856:535–357.
   Web of Science ®Google Scholar
• Asakura T, Kawai Y, Yoneyama Y, et al. Use of sodium borohydride in determination of oxygen dissociation curves of hemoglobin. Anal Biochem. 1964;7:393–400.
   PubMed Web of Science ®Google Scholar
• Olsen KW. Thermal denaturation procedures for hemoglobin. Meth Enzymol. 1994;231:514–524.
   PubMed Web of Science ®Google Scholar
• Anwised P, Kabbua T, Temsiripong T, et al. Molecular cloning and expression of α-globin and β-globin genes from crocodile (Crocodylus siamensis). Protein J. 2013;32:172–182.
   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
• Silva CJSM, Sousa F, Gübitz G, et al. Chemical modifications on proteins using glutaraldehyde. Food Technol Biotechnol. 2004;42:51–56.
   Web of Science ®Google Scholar
• Migneault I, Dartiguenave C, Bertrand MJ, et al. Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme cross-linking. BioTechniques. 2004;37:790–820.
   PubMed Web of Science ®Google Scholar
• Wu M, Feng K, Li Q, et al. Glutaraldehyde-polymerized hemoglobin and tempol (PolyHb-tempol) has superoxide dismutase activity that can attenuate oxidative stress on endothelial cells induced by superoxide anion. Artif Cells Nanomed Biotechnol. 2018;46:47–55.
   PubMed Web of Science ®Google Scholar
• Bhomia R, Trivedi V, Coleman NJ, et al. The thermal and storage stability of bovine haemoglobin by ultraviolet-visible and circular dichroism spectroscopies. J Pharm Biomed Anal. 2016;6:242–248.
   PubMed Web of Science ®Google Scholar
• Noble JE, Bailey MJA. Quantitation of protein. Meth Enzymol. 2009;463:73–95.
   PubMed Web of Science ®Google Scholar
• Saian E, Gharibshahi E, Naghavi K. Size-controlled and optical properties of monodispersed silver nanoparticles synthesized by the radiolytic reduction method. IJMS. 2013;14:7880–7896.
   Web of Science ®Google Scholar
• Hsu MC, Woody RW. The origin of the heme cotton effects in myoglobin and hemoglobin. J Am Chem Soc. 1971;93:3515–3525.
   PubMed Web of Science ®Google Scholar
• Wang Y, Zhang S, Zhang J, et al. Structural, functional and physiochemical properties of dextran-bovine hemoglobin conjugate as a hemoglobin-based oxygen carrier. Process Biochem. 2017;60:67–73.
   Web of Science ®Google Scholar
• Hargrove MS, Olson JS. The stability of holomyoglobin is determined by heme affinity. Biochemistry. 1996;35:11310–11318.
   PubMed Web of Science ®Google Scholar
• Riggs AF. The Bohr effect. Annu Rev Physiol. 1988;50:181–204.
   PubMed Web of Science ®Google Scholar
• Pace CN, Shirley BA, McNutt M, et al. Forces contributing to the conformational stability of proteins. Faseb J. 1996;10:75–83.
   PubMed Web of Science ®Google Scholar