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
2006-02-21
2006-02-21
Prouty, Rebecca E. (Department: 1652)
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...
C536S023500, C530S350000, C530S380000, C930S250000, C930S010000
Reexamination Certificate
active
07001993
ABSTRACT:
Human antithrombin variants showing a high protease inhibitory activity even in the absence of heparin wherein at least one of the amino acids at positions 78, 278, 378 and 380 in the amino acid sequence of natural human antithrombin is substituted by another amino acid. Preferable examples thereof are human antithrombin variants wherein the amino acid at position 78 is substituted by Phe; the amino acid at position 278 is substituted by Ala, Arg, Asn, Gly, His, Tyr or Val; the amino acid at position 378 is substituted by Lys, Asn or Val; and/or the amino acid at position 380 is substituted by Ala, Asp, Gly, His, lie, Leu, Asn, Pro, Arg, Thr, Tyr or Val.
REFERENCES:
patent: 5420252 (1995-05-01), Kato et al.
patent: 5618713 (1997-04-01), Zettlmeissl et al.
patent: 0 384 122 (1990-08-01), None
patent: 2-262598 (1990-10-01), None
patent: 5-339292 (1993-12-01), None
patent: 9-71600 (1997-03-01), None
patent: WO 91/00291 (1991-01-01), None
Olds R. J. et al. Anthitrombin III Budapest: a single amino acid substitution (429Pro to Leu) in a region higly conserved in the serpin family, Blood 1992, 79, 1206-1212.
Sorensen P. J. et al. Distiction of two patologic antitrombin III molecules: antithrombin III“Aalborg” and antithrombin III “Budapest”, Thromb. Res. 1982, 26, 211-219.
Fan, B., et al., “Lysine-Heparin Interactions in Antithrombin. Properties of K125M and K290M, K294M, K297M Variants,”Biochemistry,33:14156-14161 (1994).
Fitton, H. L., et al., “Five Antithrombin Variants, Four Associated with Thrombosis,”Blood Coagulation and Fibrinolysis,8:145-148 (1997).
Huntington et al.; “Mechansim of Heparin Activation of Antithrombin. Evidence for Reactive Center Loop Preinsertion With Expulsion Upon Heparin Binding”; Biochemistry, vol. 35, pp. 8495-8503, (1996).
Huntington et al.; “Conformational Conversion of Antithrombin to a Fully Activated Substrate of Factor Xa Without Need for Heparin”; Biochemistry, vol. 37, pp. 3272-3277, (1998).
Meagher et al.; “Deconvolution of the Fluorescence Emission Spectrum of Human Antithrombin and Identification of the Tryptophan Residues That are Responsive to Heparin Binding”; The Journal of Biological Chemistry, vol. 273, No. 36, pp. 23283-23289, (1998).
Shirk et al.; “Role of the H Helix in Heparin Binding to Protein C Inhibitor” ; The Journal of Biological Chemistry; vol. 269, No. 46, pp. 28690-28695, (1994).
Futamura et al.; “Serine 380 (P14)→Glutamate Mutation Activates Antithrombin as an Inhibitor of Factor Xa”; The Journal of Biological Chemistry, vol. 275, No. 6, pp. 4092-4098, (2000).
F. Tokunaga et al., Amino Acid Sequence of Porcine Antithrombin III,J Biochem,116,1164-70 (1994).
Chandra et al., Isolation and sequence characterization of a cDNA clone of human antithrombin III,Proc Natl Acad Sci,USA 80, 1845-1848 (1983).
Koide, T., Isolation and Characterization of Antithrombin III from Human, Porcine, and Rabbit Plasma, and Rat Serum,J. Biochem86, 1841-1850 (1979).
Aventis Pharma Ltd.
Finnegan Henderson Farabow Garrett & Dunner L.L.P.
Prouty Rebecca E.
Walicka Malgorzata A.
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