Abstract: Novel recombinant anticoagulation proteins, methods of their use and methods of their production are described. In particular, recombinant fusions of annexin V (ANV) and Kunitz protease inhibitors (KPI) that possess potent anticoagulant activity are provided. The fusions, abbreviated ANV:KPI, utilize ANV having high affinity for phosphatidyl-L-serine with various KPI's to target serine proteases in membrane-associated coagulation complexes in the blood coagulation cascade. ANV:KPIs are potentially useful antithrombotic drugs permitting localized passivation of thrombogenic vessel walls and associated thrombi.

Abstract: Novel recombinant anticoagulation proteins, methods of their use and methods of their production are described. In particular, recombinant fusions of annexin V (ANV) and Kunitz protease inhibitors (KPI) that possess potent anticoagulant activity are provided. The fusions, abbreviated ANV:KPI, utilize ANV having high affinity for phosphatidyl-L-serine with various KPI's to target serine proteases in membrane-associated coagulation complexes in the blood coagulation cascade. ANV:KPIs are potentially useful antithrombotic drugs permitting localized passivation of thrombogenic vessel walls and associated thrombi.

Abstract: A cDNA clone having a base sequence for human tissue factor inhibitor (TFI) has been developed and characterized and the amino acid sequence of the TFI has been determined.

Abstract: A cDNA clone having a base sequence for human tissue factor inhibitor (TFI) has been developed and characterized and the amino acid sequence of the TFI has been determined.

Abstract: A cDNA clone having a base sequence for human tissue factor inhibitor (TFI) has been developed and characterized and the amino acid sequence of the TFI has been determined.

Abstract: A cDNA clone having a base sequence for human tissue factor inhibitor (TFI) has been developed and characterized and the amino acid sequence of the TFI has been determined.

Abstract: Molecules, such as antibodies, with binding specificity for Tissue factor Inhibitor (TFI) or for polypeptides comprising one or more Kunitz domains of TFI can be used in methods to detect TFI or polypeptides containing a Kunitz domain of TFI in biological fluids. Either direct or indirect detection methods can be carried out.

Abstract: There is disclosed herein a combination of lipoprotein-associated coagulation inhibition (LACI) and sulfated polysaccharides, e.g. heparin, which exerts a synergistic anticoagulant action in whole plasma.

Abstract: A cDNA clone having a base sequence for human tissue factor inhibitor (TFI) has been developed and characterized and the amino acid sequence of the TFI has been determined. Antibodies having a binding region specific to human tissue factor inhibitor are disclosed.

Abstract: A method is disclosed for inhibiting intimal hyperplasia in a warm-blooded mammal which comprises administering topically at the site and time of a vascular injury induced by arterial intervention in said mammal a small but inhibitorily effective amount of tissue factor pathway inhibitor (TFPI) sufficient to inhibit said intimal hyperplasia.

Abstract: A pre-formed anticoagulant heparin/TFPI complex which consists of a weight ratio of at least 1.25 parts of heparin to one part of TFPI and its use in inhibiting blood cogulation.

Abstract: A cDNA clone having a base sequence for human tissue factor inhibitor (TFI) has been developed and characterized and the amino acid sequence of the TFI has been determined.

Abstract: There is disclosed a method of inhibiting fibrin dependent glomerulonephritis which comprises administering to a warm-blooded mammal a heparin/TFPI complex which consists of a weight ratio of at least 1.25 parts of heparin to one part of TFPI.

Abstract: A cDNA clone having a base sequence for human tissue factor inhibitor (TFI) has been developed and characterized and the amino acid sequence of the TFI has been determined.

Abstract: A method for reducing the extent of tissue ischemia and reperfusion injury in a warm-blooded mammal is disclosed which comprises administering by local, regional, or systemic perfusion to the site of a bodily injury subject to interval tissue ischemia in said mammal a small but effective amount of tissue factor pathway inhibitor (TFPI) sufficient to reduce the extent of said tissue ischemia and reperfusion injury.

Abstract: A cDNA clone having a base sequence for human tissue factor inhibitor (TFI) has been developed and characterized and the amino acid sequence of the TFI has been determined.

Abstract: A method for reducing the thrombogenicity of microvascular anastomoses in a warm blooded mammal comprising administering to said mammal at the site of said microvascular anastomoses contemporaneously with microvascular reconstruction of a small but inhibitory effective amount of TFPI.

Abstract: A modified t-PA having improved in vivo half-life is disclosed comprising in sequence a fibronectin finger-like domain F, a growth factor domain GF, a sequence of two K2 kringle regions and a serine protease region SP, wherein the first of said kringles is free of any glycosylation site and the second of said kringles has a single glycosylation site.

Abstract: A method is disclosed for the production of tissue factor pathway inhibitor (TFPI) which comprises expression of a non-glycosylated form of TFPI in E. coli as host and obtaining a highly active TFPI by in vitro refolding of the protein in which inclusion bodies isolated from the E. coli cells are subjected to stepwise purification comprising either series (A) or series (B) as follows:(A)(1) subjecting the inclusion bodies to sulfitolysis to form TFPI-S-sulfonate,(2) purifying TFPI-S-sulfonate by anion exchange chromatography,(3) refolding TFPI-S-sulfonate by disulfide interchange reaction, and(4) purifying active refolded TFPI by cation exchange chromatography, or(B)(1) subjecting the inclusion bodies to reduction with .beta.-mercaptoethanol in urea to form reduced TFPI,(2) purifying the reduced TFPI by cation exchange chromatography,(3) refolding reduced TFPI by disulfide interchange reaction in urea, and(4) purifying the active refolded TFPI by cation exchange chromatography.

Abstract: A method for reducing the thrombogenicity of microvascular anastomoses in a warm blooded mammal comprising administering to said mammal at the site of said microvascular anastomoses contemporaneously with microvascular reconstruction of a small but inhibitory effective amount of TFPI.