References
- Abuchowski A., Es T.V., et al. Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol. J. Biol. Chem 1977; 252: 3578–3581
- Basu A., Yang K., et al. Structure–function engineering of interferon-beta-1b for improving stability, solubility, potency, immunogenicity, and pharmacokinetic properties by site-selective mono-pegylation. Bioconjug Chem 2006; 17: 618–630
- Chang, T.M.S. 1999. Future prospects for artificial blood. Trends in Boitechnology. Tibtech, 17(2):181: 61–67.
- Chang T.M.S. Red blood cell substitutes. Best Pract Res Clin Haematol 2000; 13: 651–668
- Fronticelli C., Bucci E., Orth C. Solvent regulation of oxygen affinity in hemoglobin. J. Biol. Chem 1984; 259: 10841–10844
- Gong X.W., Wei D.Z., et al. Lowry method for the determination of pegylated proteins: the error, it reason, and a method for eliminating it. Anal Biochem 2006; 354: 157–158
- Gundersen S., Palmer A.F. Conjugation of methoxypolyethylene glycol to the surface of bovine red blood cells. Biotechnology and Bioengineering 2007; 96(6)1199–1210
- Hai T.T., Pereira D.E., et al. Surface modification of diaspirin cross-linked hemoglobin (DCLHb) with chondroitin-4-sulfate derivatives, part 1. Bioconjug Chem 2000; 11: 705–713
- Harris J.M., Zalipsky S. Poly (etylene glycol) Chemistry and Biological Applications. American Chemical Society, Washington, DC 1997
- Harris J.M., Chess R.B. Effect of pegylation on pharmaceuticals. Nat Rev Drug Discov 2003; 2: 214–21
- Hu T., Su Z.G. A solid phase adsorption method for preparation of bovine serum albumin bovine hemoglobin conjugate. Journal of Biotechnology 2003; 100: 267–275
- Israelachvili J. The different faces of poly (ethylene glycol). Proc Natl Acad Sci USA 1997; 94: 8378–8379
- Kozlowski A., Harris J.M. Improvements in protein PEGylation: pegylated interferons for treatment of hepatitis C. J. Control. Release 2001; 72: 217–224
- Kroeger K.S., Kundrot C.E. Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins. Structure 1997; 5(2)227–237
- Laemmli U.K. Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 1970; 227(259)680–685
- Lee B. K., Lee E. K., et al. Solid-phase pegylation of recombinant interferon α-2a for site-specific modification: process performance, characterization, and in vitro bioactivity. Bioconjugate Chem 2007; 18: 1728–1734
- Lu X.L., Zhao D.X., Su Z.G. Purification of hemoglobin by ion exchange chromatography in flow-through mode with PEG as an escort institute of process engineering. Artificial Cell, Blood Substitutes, and Biotechnology 2004; 32(2)209–227
- Monkarsh S.P., Spence, . Isolation of positional isomers of mono-poly (ethyleneglycol)ylated interferon-2a and the determination of their biochemical and biological characteristics. Poly(ethyleneglycol) ACS Symposium Series, J.M. Harris, S. Zalipsky, et al. American Chemical Society, Washington, DC 1997; 207–216
- Planas M., Cros E., et al. Solid-phase synthesis of new peptide–arene hybrids from N-TCP amino acids. Tetrahedron Letters 2002; 43: 4431–4434
- Winslow R.M. Hemoglobin-based Red Cell Substitutes. John Hopkins University Press, Baltimore, MD 1992; 58
- Zalipsky S., Seltzar R., Menon-Rudolph S. Evaluation of a new reagent for covalent attachment of polyethylene glycol to proteins. Biotechnol Appl Biochem 1992; 15: 100–114