Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Blood proteins or globulins – e.g. – proteoglycans – platelet...
Reexamination Certificate
2006-05-23
2006-05-23
Carlson, Karen Cochrane (Department: 1653)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Blood proteins or globulins, e.g., proteoglycans, platelet...
Reexamination Certificate
active
07049406
ABSTRACT:
The invention relates to novel recombinant hemoglobins having reduced nitric oxide scavenging and/or increased high soluble expression. The invention further relates to methods of increasing the soluble expression of recombinant hemoglobin by adding exogenous hemin in molar excess of the heme binding sites of recombinant hemoglobin.
REFERENCES:
patent: 5028588 (1991-07-01), Hoffman et al.
patent: 5428007 (1995-06-01), Fischer et al.
patent: 5449759 (1995-09-01), Hoffman et al.
patent: 5545727 (1996-08-01), Hoffman et al.
patent: 5563254 (1996-10-01), Hoffman et al.
patent: 5599907 (1997-02-01), Anderson et al.
patent: 5665869 (1997-09-01), Ryland et al.
patent: 5739011 (1998-04-01), Anderson et al.
patent: 5798227 (1998-08-01), Hoffman et al.
patent: 5801019 (1998-09-01), Anderson et al.
patent: 5843888 (1998-12-01), Ho et al.
patent: 5844088 (1998-12-01), Hoffman et al.
patent: 5844089 (1998-12-01), Hoffman et al.
patent: 5844090 (1998-12-01), Anderson et al.
patent: 5942488 (1999-08-01), Komiyama et al.
patent: 6022849 (2000-02-01), Olson et al.
patent: 6114505 (2000-09-01), Olson et al.
patent: WO 95/14038 (1995-05-01), None
patent: WO 96/40920 (1996-12-01), None
patent: WO 97/23631 (1997-07-01), None
Moore, E., et al., “Cooperativity in the Dissociation of Nitric Oxide from Hemoglobin*,”1976Journal of Biological Chemistry, vol. 251, pp. 2788-2794.
Bonaventura, J., et al., “Hemoglobin Providence—Functional Consequences of Two Alterations of the 2,3-Diphosphoglycerate Binding Site at Position β82*,” 1976 (Journal of Biolological Chemistry, vol. 251), pp. 7563-7571.
Doyle, M., et al., “Oxidation of Nitrogen Oxides by Bound Dioxygen in Hemoproteins,”1981 (Journal of Inorganic Biochemistry, vol. 14), pp. 351-358.
Fermi, G., et al., “The Crystal Structure of Human Deoxyhaemoglobin at 1-74 Å Resolution,”1984Journal of Molecular Biology, vol. 175, pp. 159-174.
White, C., et al., “Toxicity of Human Hemoglobin Solution Infused into Rabbits,” 1986 (J. Lab. Clin. Med., vol. 108), pp. 121-131.
Nagai, K., et al. “Distal Residues in the Oxygen Binding Site of Haemoglobin Studied by Protein Engineering,” 1987 (Nature, vol. 329), pp. 858-860.
Imai, K., et al. “Structural and Functional Consequences of Amino Acid Substitutions in Hemoglobin as Manifested in Natural and Artificial Mutants,” 1989 (Protein Seq. Data Anal., vol. 2), pp. 81-86.
Mitraki, A., et al. “Protein Folding Intermediates and Inclusion Body Formation,”1989 (Bio/Technology, vol. 7), pp. 690-697.
Mathews, A. J., et al., “The Effects of E7 and E11 Mutations on the Kinetics of Ligand Binding to R State Human Hemoglobin*,” 1989 (Journal of Biological Chemistry, vol. 264), pp. 16573-16583.
Lin, S. H., et al. “Effect of the Distal Residues on the Vibrational Modes of the Fe-CO Bond in Hemoglobin Studied by Protein Engineering,” 1990 (Biochemistry, vol. 29), pp. 5562-5571.
Mathews, A. J., et al. “The Assignment of Carbon Monoxide Association Rate Constants to the α and β Subunits in Native and Mutant Human Deoxyhemoglobin Tetramers*,” 1991 (Journal of Biological Chemistry, vol. 266), pp. 21631-21639.
Tame, J., et al. “Functional Role of the Distal Valine (E11) Residue of α Subunits in Human Haemoglobin,” 1991 (J. Mol. Biol., vol. 218), pp. 761-767.
Giardina, B., et al.“Protein Engineering in Haemoglobin [letter],” 1992 (Nature, vol. 355), pp. 777-778.
Looker, D., et al.—“A Human Recombinant Haemoglobin Designed for Use as a Blood Substitute,” 1992 (Nature, vol. 356), pp. 258-260.
Alayash, A., et al., “Nitric Oxide Binding to Human Ferrihemoglobins Cross-Linked Between Either α or β Subunits1,” 1993 (Archives of Biochemical Biophysics, vol. 303), pp. 332-338.
Rooney, M., et al., “Hemodilution with Oxyhemoglobin—Mechanism of Oxygen Delivery and Its Superaugmentation with a Nitric Oxide Donor (Sodium Nitroprusside),”1993 (Anesthesiology, vol. 79), pp. 60-72.
Schultz, S., et al., “A Role for Endothelin and Nitric Oxide in the Pressor Response to Diaspirin Cross-Linked Hemoglobin,”1993 (J. Lab. Clin. Med, vol. 122), pp. 301-308.
Feldman, P., et al., “The Surprising Life of Nitric Oxide,” 1993 (Chem. Eng. News, Dec.) pp. 26-38.
Fronticelli, C., et al., “The Dimer-Tetramer Equilibrium of Recombinant Hemoglobins. Stabilization of the α1β2Interface by the Mutation β(Cys112→Gly) at the α1β1Interface,” 1994 (Biophysical Chemistry, vol. 51), pp. 53-57.
Thompson, A., et al., “Stroma-Free Hemoglobin Increases Blood Pressure and GFR in the Hypotensive Rat: Role of Nitric Acid,”1994 (J. Appl. Physiol., vol. 77), pp. 2348-2354.
Hargrove, M.S., et al. “His64(E7)→Tyr Apomyoglobin as a Reagent for Measuring Rates of Hemin Dissociation*,” 1994 (J. Biol. Chem., vol. 269), pp. 4207-4214.
Looker, D., et al., “Expression of Recombinant Human Hemoglobin inEscherichia coli,” 1994 (Methods in Enzymolology, vol. 231), pp. 364-374.
Fronticelli, C., et al. “Chloride Ion Independence of the Bohr Effect in a Mutant Human Hemoglobin β (V1M=H2deleted)*,” 1994 (Journal of Biological Chemistry, vol. 269), pp. 23965-23969.
Lincoln, T.—“Protein Engineering. Hunting Haemoglobin [news; comment],” 1995Nature, vol. 373, p. 196.
Alayash, A., et al., “Hemoglobin and Free Radicals: Implications for the Development of a Safe Blood Substitute,” 1995 (Mol. Med. Today, vol. 1), pp. 122-127.
Carver & Kutlow, 1995, (International Hemoglobin Information Center Variant List Hemoglobin, vol. 19), pp. 37-149.
Militello, V., et al. “Dynamic Properties of Some β-Chain Mutant Hemoglobins,”1995 (Proteins, vol. 22), pp. 12-19.
Gould, S., et al., “Clinical Development of Human Polymerized Hemoglobin as a Blood Substitute,”1996 (World Journal of Surgery, vol. 20), pp. 1200-1207.
Eich, R. F., et al. “Mechanism of NO-Induced Oxidation of Myoglobin and Hemoglobin,” 1996 (Biochemistry, vol. 35), pp. 6976-6983.
Pechik, I., et al. “Crystallographic, Molecular Modeling, and Biophysical Characterization of the Valineβ67(E11)→Threonine Variant of Hemoglobin,” 1996 (Biochemistry, vol. 35), pp. 1935-1945.
Sanders, K. E., et al. “Engineering and Design of Blood Substitutes,” 1996 (Current Opinion in Structural Biology, vol. 6), pp. 534-540.
Kiger, L., et al. “Recombinant [Pheβ63] Hemoglobin Shows Rapid Oxidation of the β Chains and Low-Affinity, Non-Cooperative Oxygen Binding to the α Subunits,”1996 (Eur. J. Biochem., vol. 243), pp. 365-373.
Cupane, A., et al.“Modification of α-Chain or β-Chain Heme Pocket Polarity by Val(E11)→thr Substitution Has Different Effects on the Steric, Dynamic, and Functional Properties of Human Recombinant Hemoglobin. Deoxy Derivatives*” 1997 (Journal of Biological Chemistry, vol. 272), pp. 26271-26278.
Shen, T. J. , et al.“Production of Human Normal Adult and Fetal Hemoglobins inEscherichia Coli,” 1997 (Protein Engineering, vol. 10), pp. 1085-1097.
Sun, D. P., et al. “Contribution of Surface Histidyl Residues in the α-Chain to the Bohr Effect of Human Normal Adult Hemoglobin: Roles of Global Electrostatic Effects,” 1997 (Biochemistry, vol. 36), pp. 6663-6673.
Netzer, W., et al., “Recombination of Protein Domains Facilitated by Co-Translational Folding in Eukaryotes,” 1997 (Nature, vol. 388), pp. 343-349.
Olson, J., et al., “Protein Engineering Strategies for Designing More Stable Hemoglobin-Based Blood Substitutes,” 1997 (Art, Cells, Blood Subs. and Immob. Biotech., vol. 25), pp. 227-241.
Hargrove, M. S., et al. “Quaternary Structure Regulates Hemin Dissociation from Human Hemoglobin* [Pu
Doherty Daniel H
Glascock Christopher B
Lemon Douglas D
Mathews Antony J
Olson John S
Baxter Biotech Technology SARL
Carlson Karen Cochrane
Senniger Powers
William Marsh Rice University
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