Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Patent
1993-07-20
1997-10-28
Wax, Robert A.
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
435212, 4352523, 43525233, 4353201, 424 9464, 536 234, A61K 3836, C12N 1562, C12N 972, C12N 1558
Patent
active
056817215
ABSTRACT:
Bifunctional urokinase variants possessing improved fibrinolytic properties and thrombin inhibitory activities, plasmids used in the production of these polypeptides, as well as thrombolytic agents containing one of the bifunctional urokinase variants as active ingredient are described.
REFERENCES:
patent: 4751180 (1988-06-01), Cousens et al.
patent: 5002887 (1991-03-01), Larsen
patent: 5376367 (1994-12-01), Williams
Vu, T.-K. H., et al., Cell, 64: 1057-1068, 1991.
H. Thien-Khai et al., Nature, Domains Specifying Thrombin-Receptor Interaction, vol. 353, pp. 674-677, (Oct. 17, 1991).
T.C. Wun, et al., J. of Biol. Chem., Isolation and Characterization of Urokinase From Human Plasma, vol. 257, No. 6, pp. 3276-3283, (Mar. 25, 1982).
K.H. Strube, et al., J. of Biol. Chem., Isolation, Sequence Analysis and Cloning of Haemadin, vol. 268, No. 12, pp. 8590-8595, (1993).
S.-K. Yao, et al., American Physiol. Soc., Thrombin Inhibition Enhances Tissue-Type Plasminogen . . . , pp. 374-379, (1992).
S.-Y. Yue, et al., Protein Engineering, Characterization of the Interactions of a Bifunctional Inhibitor . . . , vol. 5, No. 1, pp. 77-83, (1992).
J. Robinson, et al., Tibtech, Redesigning t-PA for Improved Thrombolytic Therapy, vol. 9, pp. 86-90, (1991).
T. Rydel, et al., Reports, The Structure of a Complex of Recombinant Hirudin amd Human .alpha.-Thrombin, pp. 277-280, (Jul. 1990).
J. Schneider, Thrombosis Research, Heparin and the Thrombin Inhibitor . . . , vol. 64, No. 9, pp. 677-687, (1991).
G. Steffens, et al., Hoppe-Seyler's Z. Physiol. Chem., The Complete Amino Acid Sequence of Low Molecular Mass Urokinase from Human Urine, Bd. 363, S. 1043-1058, (Sep. 1982).
D. Stump, et al., J. of Biol. Chem., Urokinase-Related Proteins in Human Urine, vol. 261, No. 3, pp. 1267-1269, (1986).
A. Szczeklik, et al., Arteriosclerosis and Thrombosis, Persistent Generation of Thrombin After Acute Myocardial Infarction, vol. 12, No. 5, pp. 548-553, (May 1992).
U. Tebbe, et al., Z. Kardiol. 80, Suppl. 3, 32-32 (1991).
M. Mellott, et al., Arteriosclerosis and Thrombosis, Vampire Bat Salivary Plasminogen . . . , vol. 12, No. 2, pp. 212-221, (Feb. 1992).
German Abstract, DE 41 37 996, (May 27, 1993).
S. Gardell, et al., J. of Biol. Chem., Isolation, Characterization and cDNA Cloning of a Vampire Bat . . . , vol. 264, No. 30, pp. 17947-17952, (1989).
A. Gruber, et al., Circulation, Antithrombotic Effects of Combining Activated Protein C and Urokinase in Nonhuman Primates, vol. 84, No. 6, pp. 2454-2462, (Dec. 1991).
P. Eisenberg, Circulation, Balance of Procoagulant and Fibrinolytic Activity, vol. 84, No. 6, pp. 2601-2603, (Dec. 1991).
R. Flohe, Appl. Microbiol. Biotechnol, High Expression Vectors for the Production of Recombinant Single-Chain Urinary Plasminogen Activator from Escherichia coli, vol. 36, pp. 640-649, (1992).
N. Fromage, et al., Fibrinolysis, Synthesis, Purification and Biological Properties of a Truncated Mutant Form of Human Tissue Plasminogen Activator Produced in E. coli, vol. 5, pp. 187-190, (1991).
D. Collen, et al., Thrombosis and Haemostasis, Thrombolytic and Pharmacokinetic Properties of Human Tissue-Type Plasminogen Activator Variants . . . , vol. 65, No. 2, pp. 174-180, (1991).
D. Collen, et al., Blood, Basic and Clinical Aspects of Fibrinolysis and Thrombolysis, vol. 78, No. 12, pp. 3114-3124, (Dec. 15, 1991).
H.R. Lijnen, et al., Thrombosis and Haemostasis, Strategies for the Improvement of Thrombolytic Agents, vol. 66, No. 1, pp. 88-110 (1991).
J. Krstenansky, et al., J. Med. Chem., Anticoagulant Peptides . . . , vol. 30, pp. 1688-1691, (1987).
H. Heyneker et al., Genetics of Industrial Microorganisms, Expression of Human Urokinase Gene in E. coli, pp. 214-221, (1982).
H. Lijnen, et al., J. of Biol. Chem., Activation of Plasminogen by Pro-Urokinase, vol. 261, No. 3, pp. 1253-1258, (1986).
J. Maraganore, et al., Biochemistry, Design and Characterization of Hirulogs: . . . , vol. 29, pp. 7095-7101, (1990).
W. Gunzler, et al., Hoppe-Seyler's Z. Physiol. Chem., The Primary Structure of High Molecular Mass Urokinase from Human Urine, Bd. 363, S. 1155-1165, (Oct. 1992).
H. Lu, et al., Blood, Comparative Thrombolytic Properties of Bolus Injections and Continuous Infusions of a Chimeric . . . , vol. 78, No. 1, pp. 125-131, (Jul. 1, 1991).
Heinzel-Wieland Regina
Saunders Derek John
Schneider Johannes
Steffens Gerd J.
Wnendt Stephan
Gruenenthal GmbH
Moore William W.
Wax Robert A.
LandOfFree
Bifunctional urokinase variants with improved fibrinolytic chara does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Bifunctional urokinase variants with improved fibrinolytic chara, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Bifunctional urokinase variants with improved fibrinolytic chara will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-1025432