Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2007-02-06
2007-02-06
Kerr, Kathleen M. (Department: 1656)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C530S384000, C536S023100, C435S320100, C435S252300, C435S069600
Reexamination Certificate
active
10415963
ABSTRACT:
A modified factor VIIa is provided. The modified factor has increased amidolytic activity in the absence of T.F. and a higher affinity for T.F. when compared to the native factor VIIa but does not have substantially altered proteolytic activity when bound to T.F. Nucleic acid molecules that encode the factor, expression vectors that contain the nucleic acid molecules, cells that contain the nucleic acid molecules, and cells transformed with the expression vector are also provided. In a preferred embodiment, the modified factor is a human factor VIIa.
REFERENCES:
patent: 5288629 (1994-02-01), Berkner
patent: 5580560 (1996-12-01), Nicolaisen et al.
patent: 5874407 (1999-02-01), Kelley et al.
patent: 5994296 (1999-11-01), Ruf et al.
patent: 7026524 (2006-04-01), Persson et al.
patent: 2003/0096338 (2003-05-01), Pedersen et al.
patent: 2003/0130191 (2003-07-01), Persson et al.
patent: 2003/0170863 (2003-09-01), Perrsson et al.
patent: 0 200 421 (1993-07-01), None
patent: 10-58966 (1998-08-01), None
patent: 2001-061479 (2001-03-01), None
patent: WO 88/10295 (1988-12-01), None
patent: WO 94/07515 (1994-04-01), None
patent: WO 94/27631 (1994-12-01), None
patent: WO 96/12800 (1996-05-01), None
patent: WO 97/20939 (1997-06-01), None
patent: WO 98/31394 (1999-07-01), None
patent: WO 01/158935 (2001-08-01), None
patent: WO 01/75086 (2001-10-01), None
patent: WO 01/82943 (2001-11-01), None
patent: WO 01/83725 (2001-11-01), None
patent: WO 01/85198 (2001-11-01), None
patent: WO 02/22776 (2002-03-01), None
patent: WO 02/38162 (2002-05-01), None
patent: WO 02/062376 (2002-08-01), None
patent: WO 02/077218 (2002-10-01), None
patent: WO 03/027147 (2003-04-01), None
U.S. Appl. No. 10/295,682, filed Nov. 15, 2002, Persson et al.
U.S. Appl. No. 60/184,036, filed Feb. 22, 2000, Pedersen et al.
Iakhiaev, et al., “The Role of Catalytic Cleft and Exosite Residues of Factor Vlla for Complex Formation with Tissue Factor Pathway Inhibitor”,Thromb Haemostvol. 85, pp. 458-463 (2001).
Chang et al., “Engineered Recombinant Factor VII Q217Variants with Altered Inhibitor Specificities”,Biochemistry, vol. 38, pp. 10940-10948 (1999).
Mizuguchi et al., Abstract 1474, Journ of Int. Soc. Of Thromb and Haemo. Suppl.; p. 466 (Aug. 1999).
Leonard et al., Abstract 1473, Journ of Int. Soc. Of Thromb and Haemo. Suppl.; p. 466 (Aug. 1999).
Jin, “Structure-Function Study of Blood Coagulation Factor VII by In Vitro Mutagenesis and Computer Simulation”,UMI Dissertation Services, pp. ii-114 (1999).
Jin et al., “Four Loops of the Catalytic Domain of Factor VIIa Mediate the Effect of the First EGF-like Domain Substitution on FActor VIIa Catalytic Activity”,Journ of Molec Bio., vol. 307, Part. 5, pp. 1503-1517, Abstract only.
Persson et al., “Substitution of Valine for Leucine 305 in Factor VIIa Increases the Intrinsic Enzymatic Activity”,Journ of Biol Chemvol. 276 (31), pp. 29195-29199 (2001).
Peyvandi et al., “Molecular Characterization and Three-Dimensional Structural Analysis of Mutations in 21 Unrelated Families with Inherited Factor VII Deficiency”,Throm Haemost, vol. 84, pp. 250-257 (2000).
Peyvandi et al., “Two Naturally Occurring Mutations on FVII Gene (S3631-W364C) Altering Intrinsic Catalytic Activity”,Throm Haemost, vol. 88, pp. 750-755 (2002).
Stenesh J., Diet of Biochem and Molec Bio 2nd ED. p. 97 (Oct. 18, 1989).
Kumar, et al., “Specific Molecular Interaction Sites on Factor VII Involved in Factor X Activation”,Europ Journ of Biochemvol. 217 (2) pp. 509-518 (1993).
Soejima, et al., “Factor VIIa Modified in the 170 Loop Shows Enhanced Catalytic Activity but Does Not Change the Zymogen-like Property”,Journ of Bio Chem., vol. 276 (20), pp. 17229-17235 (2001).
Bernardi, et al., “Mutation Pattern in Clinically Asymptomatic Coagulation Factor VII Deficienty”,Human Mutationvol. 8 pp. 108-115 (1996).
Dickinson, et al., “Identification of Surface Residues Mediating Tissue Factor Binding and Catalytic Function of the Serine Protease Factor VIIa”Proc Natl Acad Sci USA, vol. 93, pp. 14379-14384 (96).
Neuenschwander ,et al. , Alteration of the Substrate and Inhibitor Specificities of Blood Coagulation Factor VIIa: Importance of Amino Acid Residue K191Biochemistryvol. 34 pp. 8701-8707 (1995).
Persson, et al., “Rational Design of Coagulation Factor VIIa Variants with Substantially Increased Intrinsic Activity”,Proc. Natl. Acad. Sci. vol. 98, pp. 135583-135588 (2001).
Petrovan, et al., “Residue Met156Contributes to the Labile Enzyme Conformation of Coagulation Factor VIIa”,The Journal of Biological Chemistryvol. 276, pp. 6616-6620 (2001).
Petrovan Ramona J.
Ruf Wolfram
Fitting Thomas
Kerr Kathleen M.
Schnizer Holly
The Scripps Research Institute
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