Preparation of Red Blood Cells Containing Exogenous Hemoglobin

References

• Benesch R., Benesch R. E., Yu C. I. Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. PNAS 1968; 59: 526–532
   PubMed Web of Science ®Google Scholar
• Perutz M. F., Poyart C. Bezafibrate lowers oxygen affinity of haemoglobin. The Lancet 1983; 15: 881–882
   Google Scholar
• Lalezari I., Lalezari P., Poyarat C., Marden M., Kister J., Bohn B., Fermi G., Perutz M. F. New effectors of human hemoglobin:Structure and function. Biochemistry 1990; 29: 1515–1523
   PubMed Web of Science ®Google Scholar
• Wireko D.J., Abraham F. C., Randad R. S. Allosteric modifiers of hemoglobin:2-[4[[(3,5-Disubstituted anilino)carbonyl]methyl]phenoxy]2-methylpropionic acid derivatives that lower the oxygen affinity of hemoglobin in red cell suspensions, in whole blood, and in vivo in rats. Biochemistry 1992; 31: 9141–9149
   PubMedGoogle Scholar
• Mouneimne Y., Barhoumi R., Myers T., Slogoff S., Nicolau C. Stable rightward shifts of the oxyhemoglobin dissociation curve induced by encapsulation of inositol hexaphosphate in red blood cells using electroporation. FEBS 1990; 275: 117–120
   PubMedGoogle Scholar
• Alliet D.W., Siemann K. L., Macler L. M. Manipulations in the oxygen transport capacity of blood as a means of sensitizing tumors to radiation therapy. Int. J. Radiat. Oncol. Biol. Phys. 1989; 16: 1169–1172
   PubMedGoogle Scholar
• Calais G., Hirst D. G. In situ tumor radiosensitization induced by clofibrate administration:single dose and fractionated studies. Radiother. Oncol. 1991; 22: 99–108
   PubMedGoogle Scholar
• Wood D.G., Hirst P. J., Schwartz H. C. The modification of hemoglobin affinity for oxygen and tumor radiosensitivity by antilipidemic drugs. Radial. Res. 1987; 112: 164–172
   PubMedGoogle Scholar
• Teisseire E., Stiicker O., Vicaut M-C., Villereal C., Ropars B. P., Duvelleroy M. A. Coronary response to large decreases of hemoglobin-O2 affinity in isolated rat heart. Am. J. Physiol. 1985; 249, (Heart Circ. Physiol. 18):HI 224-H1226
   Google Scholar
• Teisseire B. P., Ropars M. O., Vallez R. A., Herigault C., Nicolau C. Physiological effects of high-P50 erythrocyte transfusion on piglets. J. Appl. Physiol. 1985; 58(6)1810–1817
   PubMed Web of Science ®Google Scholar
• Lin S.R., Khandelwal R. S., Randad P. S., Meng H., et al. Enhanced oxygenation in vivo by allosteric inhibitors of hemoglobin saturation. Am. J. Physiol. 1993; 26504(Pt2)H1450–3
   Google Scholar
• Chang T. M.S. Recent and future developments in modified hemoglobin and microencapsulated hemoglobin as red blood cell substitutes. Art. Cells, Blood Subs., andlmmob. Biotech. 1997; 25: 1–24
   PubMed Web of Science ®Google Scholar
• Hahn R. D., Braun M. W., Dewhirst J.S., et al. Stroma-free human hemoglobin A decreases R3230Ac rat mammary adenocarcinoma blood flow and oxygen partial pressure. Radiat. Res. 1997; 147: 185–194
   PubMedGoogle Scholar
• De Young A.L., Kwiatkowski D., Noble R. W. Fish hemoglobins. Methods Enzymol. 1994; 211: 124–150
   Google Scholar
• Root R. W. The respiratory function of the blood of marine fishes. Biol. Bull. 1931; 61: 427–456
   Google Scholar
• Ingermann R. L. Physiological significance of Root effect hemoglobins in trout. Respir. Physiol. 1982; 49: 1–10
   PubMedGoogle Scholar
• Brunori A. Molecular adaptation to physiological requirements:the hemoglobin system of trout. Current Topics in Cellular Regulation, B.L. Horecker, E.R. Stadtman. Academic Press, NY 1975; 1–10
   Google Scholar
• Perutz M. F. Species adaptation in a protein molecular. Adv. Protein Chem. 1984; 36: 213–244
   PubMedGoogle Scholar
• Choury D., Leroux A., Kaplan J-C. Membrane-bound cytochrome b5 reductase (methemoglobin reductase) in human erythrocytes. Study in normal and methemoglobinemic subjects. JCI 1981; 67: 149–155
   PubMedGoogle Scholar
• Martin D. F., Rockwell S., Fischer J. J. Development of an in vitro assay for the survival of cells suspended from BA1112 rat sarcomas. Europ. J. Cancer Clin. Oncol. 1983; 6(19)791–797
   Google Scholar
• Zimmermann U., Riemann R., Pilwat P. Enzyme loading of electrically homogeneous human red blood cell ghosts prepared by dielectric breakdown. Biochim. Biophys. Acta 1976; 43(6)460–474
   Google Scholar
• Dale D. G., Villacorte G.L., Beutler E. High-yield entrapment of proteins into erythrocytes. Biochem. Med 1977; 18: 220–225
   PubMed Web of Science ®Google Scholar
• Dale G. L. High-efficiency entrapment of enzymes in resealed red cell ghosts by dialysis. Methods Enzymol. 1987; 149: 229–234
   PubMed Web of Science ®Google Scholar
• Sprandel A. R., Hubbard U., Chalmers R. A. In vitro studies on resealed erythrocyte ghosts as protein carriers. Res. Exp. Med. 1979; 175: 239–245
   PubMedGoogle Scholar
• De Loach J., Ihler G. A dialysis procedure for loading erythrocytes with enzymes and lipids. Biochim. Biophys. Acta 1977; 136–145; 496
   Google Scholar
• Ihler R. H., Glew G., Schnure F. W. Enzyme loading of erythrocytes. PNAS 1973; 20: 2663–2666
   Google Scholar
• Whitaker G. P., Sartiano L. J., Hamelly T.R., et al. Hypotonic exchange loading of human erythrocytes with 59Fe-labeled rabbit hemoglobins. J. Lab. Clin. Med. 1974; 84: 879–888
   Google Scholar
• Sartiano G. P., Hayes R. L. Hypotonic exchange-loading of erythrocytes. II. Introduction of hemoglobins S and C into normal red cells. J. Lab. Clin. Med. 1977; 89: 30–40
   PubMedGoogle Scholar
• Scott M. D., Rouyer-Lubin P., Fessard B. H., Beuzard Y. Entrapment of purified a-hemoglobin chains in normal erythrocytes. J. Biol. Chem. 1990; 265: 17953–17959
   PubMed Web of Science ®Google Scholar
• Brunori M., Giardina B., Chiancone E., et al. Studies on the properties offish hemoglobins. Molecular properties and interaction with third components of the isolated hemoglobins from trout (Salmo irideus). Europ. J. Biochem. 1973; 29: 563–570
   Google Scholar
• Pelster B., Weber R. E. Influence of organic phosphates on the Root effect of multiple fish haemoglobins. J. Exp. Biol. 1990; 149: 425–437
   Google Scholar
• Noble L. D., Kwiatkowski R.W., De Young A., et al. Functional properties of hemoglobins from deep-sea fish:correlations with depth distribution and presence of a swimbladder. Biochim. Biophy. Acta 1986; 870: 552–563
   PubMedGoogle Scholar