No-modified hemoglobins and uses therefor

Details No-modified hemoglobins and uses therefor No-modified hemoglobins and uses therefor

2007-04-10

2007-04-10

Lukton, David (Department: 1654)

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...

C514S006900, C536S026250, C436S066000

Reexamination Certificate

active

10638969

ABSTRACT:
Nitrosylhemoglobin can be produced by introducing gaseous NO into an aqueous solution of hemoglobin. It has been demonstrated that nitrosylhemoglobin in aqueous solution can be converted to SNO-hemoglobin upon introduction of oxygen to the solution, as is postulated to occur in the lungs. Nitrosylhemoglobin can be used in methods to produce the physiological effects of NO, for example, to reduce vasoconstriction and to inhibit platelet aggregation.

REFERENCES:
patent: 5044435 (1991-09-01), Sperl et al.
patent: 5077208 (1991-12-01), Sublette
patent: 5427797 (1995-06-01), Frostell et al.
patent: 5591710 (1997-01-01), Hsia
patent: 6153186 (2000-11-01), Stamler et al.
patent: 6203789 (2001-03-01), Stamler et al.
patent: 6255277 (2001-07-01), Stamler et al.
patent: 6291424 (2001-09-01), Stamler et al.
patent: 6471978 (2002-10-01), Stamler et al.
patent: 6583113 (2003-06-01), Stamler et al.
patent: 2002/0037839 (2002-03-01), Stamler et al.
patent: 2002/0052314 (2002-05-01), Stamler et al.
patent: 2003/0007967 (2003-01-01), Stamler et al.
patent: 2003/0022267 (2003-01-01), Stamler et al.
patent: 2003/0072783 (2003-04-01), Stamler et al.
patent: 2003/0211977 (2003-11-01), Stamler et al.
patent: 2004/0132638 (2004-07-01), Stamler et al.
patent: WO 93/09806 (1993-05-01), None
patent: WO 94/22306 (1994-10-01), None
patent: WO 94/22482 (1994-10-01), None
patent: WO 94/22499 (1994-10-01), None
patent: WO 96/30006 (1996-10-01), None
patent: WO 97/18000 (1997-05-01), None
patent: WO 97/37664 (1997-10-01), None
Mooji (Contraception 44, 277, 1991).
Suzuki M., Experimental animals / Japanese Association for Laboratory Animal Science 48 (3) 199-202, 1999.
Feder (Journal of Nutrition 121, 72-79, 1991).
Torres (Journal of Inorganic Biochemistry 66(3), 207-212, 1977).
Hess, J. R. (Seminars in Hematology 33(4), 369-78, 1996).
Simon, D.I., et al., “Polynitrosylated Proteins: Characterization, Bioactivity, and Functional Consequences,”Proc. Natl. Acad. Sci. USA, 93:4736-4741 (1996).
Doyle, M.P., et al., “Structural Effects in Alkyl Nitrite Oxidation of Human Hemoglobin,”Journal of Biological Chemistry, 259(1): 80-87 (1984).
Shah, N.S., et al., “Efficacy of Inhaled Nitric Oxide in a Porcine Model of Adult Respiratory Distress Syndrome,”Archives of Surgery, 129(2): 158-164 (1994).
Olsen, S.B., et al., “Enhancement of Platelet Deposition by Cross-linked Hemoglobin in a Rat Carotid Endarcterectomy Model,”Circulation, 93(2): 327-332 (1996).
Wheeler, G.P., et al., “Anti-Sickling Activity of Nitrosoureas,”Biochem. Biophys. Res. Comm., 54(3): 1024-1029 (1973).
Stamler, J.S., “Redox Signaling: Nitrosylation and Related Target Interactions of Nitric Oxide,”Cell, 78:931-936 (1994).
Arnelle, D.R., et al., “NO+, NO., and NO−Donation by S-Nitrosothiols: Implications for Regulation of Physiological Functions by S-Nitrosylation and Acceleration of Disulfide Formation,”Archives of Biochemistry and Biophysics, 318(2): 279-285 (1995).
Jia, L., et al., “S-Nitrosohaemoglobin: A Dynamic Activity of Blood Involved in Vascular Control,”Nature, 380:221-226 (1996).
Ignarro, L.J., et al., “Mechanism of Vascular Smooth Muscle Relaxation by Organic Nitrates, Nitrites, Nitroprusside and Nitric Oxide: Evidence for the Involvement of S-Nitrosothiols as Active Intermediates,”The Journal of Pharmacology and Experimental Therapeutics, 218(3): 739-749 (1981).
Ribeiro, J.M.C., et al., “Reversible Binding of Nitric Oxide by a Salivary Heme Protein from a Bloodsucking Insect,”Science, 260:539-541 (1993).
Scharfstein, J.S., et al., “In VivoTransfer of Nitric Oxide Between a Plasma Protein-Bound Reservoir and Low Molecular Weight Thiols,”J. Clin. Invest., 94:1432-1439 (1994).
Kruszyna, R., et al., “Generation of Valency Hybrids and Nitrosylated Species of Hemoglobin in Mice by Nitric Oxide Vasodilators,”Toxicol. Appl. Pharmacol., 94(3): 458-465 (1988).
Greenburg, A.G., et al., “Nitrosyl Hemoglobin FormationIn VivoAfter Intravenous Administration of a Hemoglobin-Based Oxygen Carrier in Endotoxemic Rats,”Artif. Cells, Blood Substitutes, Immobilization Biotechnol., 23(3): 271-276 (1995).
Sharma, V.S. et al., “The Dissociation of NO from Nitrosylhemoglobin,”J. Biol. Chem., 253(18): 6467-6472 (1978).
Moore, E.G., et al., “Cooperativity in the Dissociation of Nitric Oxide from Hemoglobin,”J. Biol. Chem., 251(9): 2788-2794 (1976).
Khartitonov, V.G. et al., “Interactions of Nitric Oxide with Heme Proteins Using UV-VIS Spectroscopy,”Methods in Nitric Oxide Research, pp. 39-45, Edited by Martin Feelisch and Jonathan S. Stamler, John Wiley & Sons Ltd. (1996).
Taketa, F., et al., “Chain Nonequivalence in Binding of Nitric Oxide to Hemoglobin,”J. Biol. Chem., 253(15): 5448-5451 (1978).
Henry, Y., et al., “Chain Non-Equivalence in Nitric Oxide Binding to Hemoglobin,”Biochem. and Biophys. Res. Comm., 51(3): 659-665 (1973).
Wennmalm, A., et al., “Dependence of the Metabolism of Nitric Oxide (NO) in Healthy Human Whole Blood on the Oxygenation of its Red Cell Haemoglobin,”Br. J. Pharmacol., 106: 507-508 (1992).
Cassoly, R., et al., “Conformation, Co-Operativity and Ligand Binding in Human Hemoglobin,”J. Mol. Biol., 91: 301-313 (1975).
Cantilena, L.R., Jr., et al., “Nitric Oxide Hemoglobin in Patients Receiving Nitroglycerin as Detected by Electron Paramagnetic Resonance Spectroscopy,”J. Lab. Clin. Med., 120(6): 902-907 (1992).
Kruszyna, H., et al., “Red Blood Cells Generate Nitric Oxide From Directly Acting, Nitrogenous Vasodilators,”Toxicology and Applied Pharmacology, 91: 429-438 (1987).
Wade, R.S., et al., “Redox Reactivity of Iron (III) Porphyrins and Heme Proteins with Nitric Oxide: Nitrosyl Transfer to Carbon, Oxygen, Nitrogen and Sulfur,”Chem. Res. Toxicol., 3(4):289-291 (1990).
Perutz, M.F., et al., “Influence of Globin Structures on the State of the Heme: Ferrous Low Spin Derivatives,”Biochemistry, 15(2): 378-387(1976).
Butler, A.R., et al., “NO, Nitrosonium Ions, Nitroxide Ions, Nitrosothiols and Iron-Nitrosyls in Biology: A Chemist's Perspective,”TiPS, 16: 18-22 (1995).
Kumura, E., et al., “Nitrosyl Hemoglobin Production During Reperfusion After Focal Cerebral Ischemia in Rats,”Neuroscience Letters, 177: 165-167 (1994).
Shiga, T., et al., “Electron Paramagnetic Resonance Studies of Nitric Oxide Hemoglobin Derivatives: I. Human Hemoglobin Subunits,”Biochemistry, 8: 378-383 (1969).
Garel, M.C., et al., “Binding of 21 Thiol Reagents to Human Hemoglobin in Solution and in Intact Cells,”Eur. J. Biochem., 123: 513-519 (1982).
Garel, M.C., et al., “Covalent Binding of Glutathione to Hemoglobin: I. Inhibition of Hemoglobin S Polymerization,”J. Biol. Chem., 261(3): 14704-14709 (1986).
Gow, A.J., et al., “Reactions Between Nitric Oxide and Haemoglobin Under Physiological Conditions,”Nature, 391: 169-173 (1998).
Feelisch, M., et al., “Understanding the Controversy Over the Identity of EDRF,”Nature, 368: 62-65 (1994).
Moriguchi, M., et al., “Nitric Oxide Can Modify Amino Acid Residues in Proteins,”Biochem. Biophys. Res. Comm., 183(2): 598-604 (1992).
Doyle, M.P., et al., “Oxidation of Nitrogen Oxides by Bound Dioxygen in Hemoproteins,”J. Inorganic Biochem., 14: 351-358 (1981).

Affiliated with

Also associated with

Rating

No-modified hemoglobins and uses therefor does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with No-modified hemoglobins and uses therefor, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and No-modified hemoglobins and uses therefor will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3783727