Process for production of inhibited forms of activated blood fac

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...

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435 681, 530384, 530413, 530829, C07K 14745, C07K 118, A61K 3836, C12P 2106

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active

056022336

ABSTRACT:
A process for producing a highly purified preparation of an inhibited form of an activated blood factor entails providing a partially purified preparation containing the blood factor of interest, treating the partially purified preparation to convert the blood factor to an inhibited activated form in a single step, and then purifying the resulting inhibited activated blood factor.

REFERENCES:
patent: 4285932 (1981-08-01), Smith
patent: 4318904 (1982-03-01), Shaw et al.
patent: 4337244 (1982-06-01), Smith
patent: 4447416 (1984-05-01), Menache-Aronson
patent: 4604285 (1986-08-01), Smith et al.
patent: 4721572 (1988-01-01), Jordan
patent: 4725673 (1988-02-01), Herring
patent: 5071961 (1991-12-01), Kraus et al.
patent: 5120537 (1992-06-01), Esmon et al.
patent: 5153166 (1992-10-01), Jain et al.
patent: 5153175 (1992-10-01), Krueger et al.
patent: 5278144 (1994-01-01), Wolf
patent: 5279956 (1994-01-01), Griffin et al.
Ahmad, et al., "Rapid Purification of Factor IX, Factor X and Prothrombin by Immunoaffinity and Ion Exchange Chromatography," Thrombosis Research (1989) 55:121-133.
Aronson, et al., "Two Forms of the Human Prothrombin Converting Enzyme (Active Factor X) (35769)," Two Forms of X, (1971) 137:4, 1262-1266.
Bajaj, et al., "A Simplified Procedure for Purification of Human Prothrombin, Factor IX and Factor X," Preparative Biochemistry (1981) 11:4, 397-412.
Bauer, et al, "Detection of Factor X Activation in Humans," Blood (1989) 74:6 (Nov. 1), 2007-2015.
Benedict, et al., "Active Site-Blocked Factor Xa Prevents Thrombus Formation in the Coronary Vasculature in Parallel With Inhibition of Extravascular Coagulation in a Canine Thrombosis Model," Blood (1993) 81:8, 2059-2066.
Cassels, et al., "The Interaction of Streptokinase Plasminogen Activator Complex Tissue-Type Plasminogen Activator, Urokinase and their Acylated Derivatives with Fibrin and Cyanogen Bromide Digest of Fibrinogen," Biochem. J. (1987) vol. 247, 395-400.
Chattopadhyay, et al., "Molecular Recognition in the Activation of Human Blood Coagulation Factor X," The Journal of Biological Chemistry, (1989) 264:19, 11035-11043.
Claeson, "Synthetic Peptides and Peptidomimetics as Substrates and Inhibitors of Thrombin and Other Proteases in the Blood Coagulation System," Blood Coagulation and Fibrinolysis (1994) 5, 411-436.
Colman, et al., "Section A, Plasma Coagulation Factors," Plasma Coagulation Factors, 3-17.
Crabbe, et al., "Acylated Plasminogen-Streptokinase Activator Complex: A New Approach to Thrombolytic Therapy," Pharmacotherapy (1990) 10:2, 115-126.
Davie, "Chapter 16, The Blood Coagulation Factors: Their cDNAs, Genes, and Expression," Plasma Coagulation Factors, Part 1, Section A, 242-268.
Di Scipio, et al., "Activation of Human Factor X (Stuart Factor) by a Protease from Russell's Viper Venom, Activation of Human Factor X," Biochemistry (1977) 16:24, 5253-5260.
Etingin, et al., "Viral Activation of the Coagulation Cascade: Molecular Interactions at the Surface of Infected Endothelial Cells," Cell (1990) 61:657-662.
Fears, "Development of Anisoylated Plasminogen-Streptokinase Activator Complex from the Acyl Enzyme Concept," Seminars in Thrombosis and Hemostasis (1980) 15:2, 129-139.
Fears, et al., "The Protective Effect of Acylation on the Stability of Anisoylated Plasminogen Streptokinase Activator Complex in Human Plasma," Drugs (1987) 33 (Suppl. 3), 57-63.
Friedberg, et al., "Large Scale Purification of Factor X by Hydrophobic Chromatography," Preparative Biochemistry (1988) 18:3, 303-320.
Furie, et al., "Coagulant Protein of Russell's Viper Venom," Blood Clotting Enzymes, Methods in Enzymology, (1976) 45, 191-205.
Furie, et al., "The Molecular Basis of Blood Coagulation," Cell (1988) 53:505-518.
Gordon, et al., "The Site of Activation of Factor X by Cancer Procoagulant," Blood Coagulation and Fibrinolyses (1991) 2:735-739.
Hoover, et al., "The Adhesive Interaction between Polymorphonuclear Leukocytes and Endothelial Cells in Vitro," Cell (1978) 14:423-428.
Hrinda, et al., "Preclinical Studies of a Monoclonal Antibody-Purified Factor IX, Mononinep.TM." Seminars in Hematology (1991) 28:3, Suppl. 6 (Jul.), 6-14.
Jesty, "Analysis of the Generation and Inhibition of Activated Coagulation Factor X in Pure Systems and in Human Plasma," The Journal of Biological Chemistry (1986) 261:19, 8695-8702.
Kettner, et al, "Synthesis of Peptides of Arginine Chloromethyl Ketone. Selective Inactivation of Human Plasma Kallikrein," Biochemistry, (1978) 17:22, 4778-4783.
Kettner, et al., "The Susceptibilty of Urokinase to Affinity Labeling by Peptides of Arginine Chloromethyl Ketone," Biochimica et Biophysica Acta (1979) 569:31-40.
Kettner, et al., "Active Site Mapping of Human and Rat Urinary Kallikreins by Peptidyl Cholormethyl Ketones," Archives of Biochemistry and Biophysics (1980) 202:2, 420-430.
Kettner, et al., "Inactivation of Trypsin-Like Enzymes with Peptides of Arginine Chloromethyl Ketone," Methods in Enzymology (1981) 80:826-842.
Kettner, et al., "The Selective Affinity Labeling of Factor X.sub.a by Peptides of Arginine Chloromethyl Ketone," Thrombosis Research (1981) 22:645-652.
Kosow, "Purification and Activation of Human Factor X: Cooperative Effect of Ca.sup.++ on the Activation Reaction," Thrombosis Research (1976) 9:565-573.
Lijnen, et al., "Inhibition of Tryspin-Like Serine Proteinases by Tripeptide Arginyl and Lysyl Chloromethylketones," Thrombosis Research (1984) 34:431-437.
Marsh, "Snake Venoms Affecting the Haemostatic Mechanism--a Consideration of their Mechanisms Practical Applications and Biological Significance," Blood Coagulation and Fibrnolysis (1994) 5:399-410.
Mertens, et al., "Pathways in the Activation of Human Coagulation Factor X," Biochem. J. (1980) 185:647-658.
Miletich, et al., "The Synthesis of Sulfated Dextran Beads for Isolation of Human Plasma Coagulation Factors II, IX and X," Analytical Biochemistry, (1980) 105:304-310.
Monahan, et al., "Identification of Human Cohn Fraction III as a Useful Source for the Simultaneous Purification of FIX and FX Zymogens, " Thrombosis Research (1980) 19:743-755.
Nesheim, et al., "The Contribution of Bovine Factor V and Factor Va to the Activity of Prothrombinase," The Journal of Biological Chemistry (1979) 254:21, 10952-10962.
Nesheim, et al., "Cofactor Dependence of Factor Xa Incorporation into the Prothrombinase Complex," The Journal of Biological Chemistry (1981) 256:13, 6537-6540.
Sinha, et al., "Procoagulation Activities of Reversibly Acylated Forms of Factor Xa," Blood, (1995) 86:4153-4157.
Steinberg, et al., "Activation of Factor X", Plasma Coagulation Factors, Part 1, Section A, Chapter 7, 112-119.
Sturzebecker, J., et al., "Acyl-Derivatives of tPA," Thrombosis Research (1987) 47:6, 699-703 (first page missing).
Williams, et al., "Zymogen/Enzyme Discrimination Using Peptide Chloromethyl Ketones," The Journal of Biological Chemistry (1989) 264:13, 7536-7545.

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