Low oxygen affinity mutant hemoglobin

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

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530385, 435 691, C07K 14805, C07H 2106

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active

058438882

ABSTRACT:
A non-naturally occurring mutant hemoglobin (.alpha.96Val.fwdarw.Trp) is provided that has a lower oxygen affinity than that of native hemoglobin, but high cooperativity in oxygen binding. The mutant hemoglobin is preferably obtained by recombinant DNA techniques. Such a mutant hemoglobin may be used as a component of a blood substitute.

REFERENCES:
patent: 4865974 (1989-09-01), Ben-Bassat et al.
patent: 4870017 (1989-09-01), Ben-Bassat et al.
patent: 5013662 (1991-05-01), Ben-Bassat et al.
patent: 5028588 (1991-07-01), Hoffman et al.
Ho et al. 1994 Biophys. T. 66 (2pt2): A269.
Tame et al 1991 J Mol. Biol 218: 761-767.
Kim et al 1995 J. Mol. Biol 248(1): 867-882.
Mulder, A.G., et al., J. Cell. Comp. Physiol. 5:383 (1934).
Bunn, H.F., et al., J. Exp. Med. 129:909 (1969).
Chada, K., et al., Nature (London) 314:377 (1985).
Townes, T.M., et al., EMBO J. 4:1715 (1985).
Swanson, M.E., et al., Bio/Technology 10:557 (1992).
Groebe, D.R., et al., Protein Expression and Purification 3:134 (1992).
Wagenbach, M., et al., Bio/Technology 9:57 (1991).
DeLlano, J.J., et al., Proc. Natl. Acad. Sci. USA 90:918 (1993).
Hoffman, S.J., et al., Proc. Natl. Acad. Sci. USA 87:8521 (1990).
Hernan, R.A., et al., Biochemistry 31:8619 (1992).
Shen, T.-J., et al., Proc. Natl. Acad. Sci. USA 90:8108 (1993).
Nagai, K., et al., Nature (London) 309:810 (1984).
Nagai, K., et al, Methods Enzymol. 153:461 (1987).
Bunn, H.F., et al., Hemoglobin: Molecular, Genetic and Clinical Aspects (Saunders, Philadelphia) pp. 37-60 (1986).
Kavanaugh, J.S., et al., Biochemistry 31:8640 (1992).
Ben-Bassat, A., et al., J. Bacteriol. 169:751 (1987).
Dickerson, R.E., et al., Hemoglobin: Structure, Function, Evolutiion, and Pathology, (The Benjamin Cummings Publishing Co., Menlo Park, CA) (1983).
Bunn, H.F., et al., J. Biol. Chem. 249:7402 (1974).
Perutz, M.F., et al., Mechanisms of Cooperativity and Allosteric Regulation in Proteins, Cambridge University Press (1990).
Reed, C.S., et al. Blood 31:623 (1968).
Jones, R.T., et al., J. Clin. Invest. 46:1840 (1967).
Weatherall, D.J., et al., British J. Haematol. 35:177 (1977).
Fermi, G., et al., J. Mol. Biol. 175:159 (1984).
Ishimori, K., et al., J. Biol. Chem. 264:14624 (1989).
Imai, K., et al., J. Mol. Biol. 218:769 (1991).
Shaanan, B., et al., J. Mol. Biol. 171:31 (1983).
Schneider, R.G., et al., Biochim. Biophys. Acta. 400:365 (1975).
Bonaventura, J., et al., J. Biol. Chem. 243:980 (1968).
Moo-Penn, W.F., et al., FEBS Lett. 92:53 (1978).
O'Donnell, J.K., et al., J. Biol. Chem. 269:27692 (1994).
Baudin, V., et al., Biochim. Biophys. Acta. 1159:223 (1992).
Dang, L.X., et al., J. Am. Chem. Soc. 111:8505 (1989).
Gao, J., et al., Science 244:1069 (1989).
Kim, H.-W., et al., Proc. Natl. Acad. Sci. USA 91:11547 (1994).
Kunkel, T.M., et al., Proc. Natl. Acad. Sci. USA 82:488 (1985).
Antonini, E., et al., Hemoglobin and Myoglobin in Their Reactions with Ligands (North Holland, Amsterdam) p. 19 (1971).
Lindstrom, T.R., et al., Proc. Natl. Acad. Sci. USA 69:1707 (1972).
Hewick, R.M., et al., J. Biol. Chem. 256:7990 (1981).
Pure Appl. Chem. 63:975 (1991).
Bunn, H.F., et al., Hemoglobin: Molecular, Genetic and Clinical Aspects (W.P. Saunders, Inc., Philadelphia, PA) pp. 634-662 (1986).
Ho, C., Adv. Protein Chem. 43:153 (1992).
Plateau, P., et al., J. Am. Chem. Soc. 104:7310 (1982).
Hayashi, A., et al., Biochim. Biophys. Acta 310:309 (1973).
Brooks, C.L., et al., J. Mol. Biol. 208:159 (1989).
Jorgensen, W.L., et al., J. Chem. Phys. 79:926 (1983).
Ponder, J.W., et al., J. Mol. Biol. 193:775 (1987).
Tidor, B., et al., Biochemistry 30:3217.
Ryckaert, J.-P., et al., J. Comput. Phys. 23:327 (1977).
Kirkwood, J.G., J. Chem. Phys. 3:300 (1935).
Brooks, C.L., et al., J. Phys. Chem. 90:6680 (1986).
Lindstrom, T.R., et al., Biochemistry 11:1677 (1972).
Dalvit, C., et al., Biochemistry 24:3398 (1985).
Takashashi, S., et al., Biochemistry 19:5196 (1980).
La Mar, G.N., et al., Biochem. Biophys. Res. Commun. 96:1172 (1980).
Fung, L.W.-M., et al., Biochemistry 14:2526 (1975).
Jesson, J.P., J. Chem. Phys. 47:579 (1967).
Kurland, R.J., et al., J. Magn. Reson. 2:286 (1970).
Johnson, M.E., et al., J. Am. Chem. Soc. 99:1245 (1977).
Turner, G.J., et al., Proteins 14:133 (1992).
Winslow, R.M., et al., eds. Blood Substitutes Physiological Basis of Efficacy (Birkauser, Boston, MA) pp. 82-84 (1995).
Manning, L.R., et al., Biochemistry 27:6640 (1988).
Benesch, R.E., et al., Biochem. Biophys. Res. Comm. 156:9 (1988).
Bucci, E., et al., J. Biol. Chem. 264:6191 (1989).
Chang, T.M.S., et al., eds. Proceeding of II International Symposium on Blood Substitutes, Biomater. Artif. Cells Artif. Organs (1988).
Kluger, R., et al., Biochemistry 31:7551 (1992).
DeVenuto, F., et al., Surg. Gynecol. Obstet. 155:342 (1982).

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