Identification
- Summary
Coagulation Factor IX Human is a coagulation factor used to treat hemophilia B or factor IX hemophilia.
- Brand Names
- Alphanine Sd, Balfaxar, Beriplex, Immunine Vh, Kcentra, Octaplex
- Generic Name
- Coagulation Factor IX Human
- DrugBank Accession Number
- DB13152
- Background
Factor IX (or Christmas factor) is one of the serine proteases of the coagulation system; it belongs to peptidase family S1. Deficiency of this protein causes hemophilia B.
- Type
- Biotech
- Groups
- Approved
- Biologic Classification
- Protein Based Therapies
Blood factors - Protein Structure
- Protein Chemical Formula
- C2041H3136N558O641S25
- Protein Average Weight
- 46548.2 Da
- Sequences
>DB00100 sequence YNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGG SCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAEN QKSCEPAVPFPCGRVSVSQTSKLTRAEAVFPDVDYVNSTEAETILDNITQSTQSFNDFTR VVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEE TEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFL KFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDS CQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
Download FASTA Format- Synonyms
- Antihemophilic factor B
- Coagulation factor IX (human)
- Factor IX (Human)
- Factor IX purificado
- Human coagulation factor IX
Pharmacology
- Indication
Factor IX is used to treat Christmas disease. Factor IX deficiency is treated by injection factor IX produced from human plasma. Tranexamic acid may be of value in patients undergoing surgery who have inherited factor IX deficiency in order to reduce the perioperative risk of bleeding.
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- Contraindications & Blackbox Warnings
Prevent Adverse Drug Events TodayTap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.Avoid life-threatening adverse drug events with our Clinical API- Pharmacodynamics
Binds vitamin K and factor VIIIa. Cleaves the Arg-Ile bond in factor X to form active factor Xa. Plays a key role in blood coagulation and clotting. Injections of factor IX are used to treat hemophilia B, which is sometimes called Christmas disease. AlphaNine is injected to increase plasma levels of Factor IX and can temporarily correct this coagulation defect. The activated partial thromboplastin time (aPTT) is prolonged in people with hemophilia B. Treatment with factor IX concentrate may normalize the aPTT by temporarily replacing the factor IX. The administration of BeneFIX increases plasma levels of factor IX, and can temporarily correct the coagulation defect in these patients.
- Mechanism of action
Coagulation Factor IX is an important protein in the process of hemostasis and normal blood clotting as it plays a key role within the coagulation cascade. It is located within the blood plasma as a zymogen, an antecedent to enzymatic function, in its inactivated state. Factor IX is dependent on the presence of Vitamin K, and is activated to a serine protease by the function of Coagulation Factor XIa. Factor XIa cleaves the peptide bond associated with protein activation in Factor IX, leaving Factor IX with two exposed chains, a light chain and a heavy chain. These two chains are held together by several disulfide bonds that reinforce the structure of Factor IX's activated form. After being activated, Factor IX forms a complex with calcium ions, membrane phospholipids and Coagulation Factor VIII to activate Coagulation Factor X. The activation of Factor X then performs a similarly integral step in the blood coagulation cascade. The ultimate result of phenotypically normal coagulation factors is the creation of platelets for normal blood clotting.
Target Actions Organism ACoagulation factor X activatorHumans ACoagulation factor XI ligandHumans ACoagulation factor VII ligandHumans ACoagulation factor VIII cofactorHumans UProthrombin Not Available Humans UProlow-density lipoprotein receptor-related protein 1 Not Available Humans UVitamin K-dependent gamma-carboxylase Not Available Humans - Absorption
Not Available
- Volume of distribution
Not Available
- Protein binding
Not Available
- Metabolism
- Not Available
- Route of elimination
Not Available
- Half-life
18.8 ± 5.4 hours.
- Clearance
8.62 ± 1.7.
- Adverse Effects
Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.- Toxicity
Not Available
- Pathways
- Not Available
- Pharmacogenomic Effects/ADRs Browse all" title="About SNP Mediated Effects/ADRs" id="snp-actions-info" class="drug-info-popup" href="javascript:void(0);">
- Not Available
Interactions
- Drug Interactions Learn More" title="About Drug Interactions" id="structured-interactions-info" class="drug-info-popup" href="javascript:void(0);">
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
Drug Interaction Integrate drug-drug
interactions in your softwareAbciximab The therapeutic efficacy of Coagulation Factor IX Human can be decreased when used in combination with Abciximab. Acenocoumarol The therapeutic efficacy of Coagulation Factor IX Human can be decreased when used in combination with Acenocoumarol. Alpha-1-proteinase inhibitor Alpha-1-proteinase inhibitor may increase the thrombogenic activities of Coagulation Factor IX Human. Alteplase The therapeutic efficacy of Coagulation Factor IX Human can be decreased when used in combination with Alteplase. Aminocaproic acid The risk or severity of adverse effects can be increased when Aminocaproic acid is combined with Coagulation Factor IX Human. - Food Interactions
- No interactions found.
Products
Drug product information from 10+ global regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.- Brand Name Prescription Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image Bebulin Kit 30 [iU]/1mL Intravenous Baxalta Incorporated 1992-08-19 2018-11-30 US 
Bebulin VH Kit 300 [iU]/1mL Intravenous Baxter Laboratories 2011-03-16 2012-09-30 US Immunine Vh Powder, for solution 720 unit / 5 mL Intravenous Takeda 1996-10-18 Not applicable Canada 
Mononine Injection, powder, lyophilized, for solution 100 [iU]/1mL Intravenous CSL BEHRING LLC 1992-08-20 2009-04-06 US Mononine Kit 1000 [iU]/10mL Intravenous CSL BEHRING LLC 1992-08-20 2022-01-28 US - Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image AlphaNine SD Coagulation Factor IX Human (1000 [iU]/10mL) + Water (1 mL/1mL) Kit Intravenous GRIFOLS USA, LLC 1990-12-31 Not applicable US AlphaNine SD Coagulation Factor IX Human (500 [iU]/10mL) + Water (1 mL/1mL) Kit Intravenous GRIFOLS USA, LLC 1990-12-31 Not applicable US AlphaNine SD Coagulation Factor IX Human (1500 [iU]/10mL) + Water (1 mL/1mL) Kit Intravenous GRIFOLS USA, LLC 1990-12-31 Not applicable US AlphaNine SD Coagulation Factor IX Human (1000 [iU]/10mL) + Water (1 mL/1mL) Kit Intravenous GRIFOLS USA, LLC 1990-12-31 2020-03-31 US AlphaNine SD Coagulation Factor IX Human (500 [iU]/10mL) + Water (1 mL/1mL) Kit Intravenous GRIFOLS USA, LLC 1990-12-31 2018-10-21 US - Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image REBLENINE VF 500 IU FAKTOR IX FLAKON, 1 ADET Coagulation Factor IX Human (500 IU/10ml) Injection, powder, lyophilized, for solution Intravenous VİTALİS SAĞLIK ÜRÜNLERİ DANIŞMANLIK VE TİC. A.Ş. 2015-09-29 Not applicable Turkey 
Categories
- ATC Codes
- B02BD04 — Coagulation factor ix
- B02BD — Blood coagulation factors
- B02B — VITAMIN K AND OTHER HEMOSTATICS
- B02 — ANTIHEMORRHAGICS
- B — BLOOD AND BLOOD FORMING ORGANS
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- Not Available
- Kingdom
- Organic Compounds
- Super Class
- Organic Acids
- Class
- Carboxylic Acids and Derivatives
- Sub Class
- Amino Acids, Peptides, and Analogues
- Direct Parent
- Peptides
- Alternative Parents
- Not Available
- Substituents
- Not Available
- Molecular Framework
- Not Available
- External Descriptors
- Not Available
- Affected organisms
- Not Available
Chemical Identifiers
- UNII
- 6U90Y1795T
- CAS number
- 181054-95-5
References
Clinical Trials
- Clinical Trials Learn More" title="About Clinical Trials" id="clinical-trials-info" class="drug-info-popup" href="javascript:void(0);">
Phase Status Purpose Conditions Count 4 Completed Not Available Hemophilia B 1 4 Completed Other Arrhythmia / Blood Platelet Transfusion / Cardiac Diseases / Cardiopulmonary Bypass / Death / Surgery, Cardiac 1 4 Completed Prevention Coronavirus Disease 2019 (COVID‑19) / Hemophilia B 1 4 Completed Treatment Bleeding / Blood Loss During Surgery / Cardiovascular Surgical Procedures / Fresh Frozen Plasma / Prothrombin Complex Concentrates 1 4 Completed Treatment Hemophilia B 2
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
Form Route Strength Injection Intravenous 800 UI Injection, powder, for solution Intravenous 200 UI Injection, powder, for solution Intravenous 500 UI Injection, powder, for solution Intravenous 800 UI Powder, for solution Intravenous 1000 U.I. Powder, for solution Intravenous 200 U.I./5ML Powder, for solution Intravenous 500 U.I. Injection, solution Intravenous 500 IU/10mL Injection, powder, for solution Intravenous 100 IU Injection, powder, for solution Intravenous 1500 IU/10ML Injection, solution Intravenous 1000 U.I. Injection, solution Intravenous 500 U.I. Powder, for solution Parenteral 1000 U.I. Powder, for solution Parenteral 1500 U.I. Powder, for solution Parenteral 500 U.I. Injection, powder, lyophilized, for solution Intravenous 50 IU Kit Intravenous Injection, powder, for solution Intravenous 1000 IU/10ml vial Injection, powder, for solution Intravenous 1500 IU/10ml vial Injection, powder, for solution Intravenous 500 IU/10ml vial Kit Intravenous 30 [iU]/1mL Kit Intravenous 300 [iU]/1mL Injection, powder, for solution Intravenous; Parenteral 1500 IU Injection, powder, for solution Intravenous; Parenteral 250 IU Injection, powder, for solution Parenteral 1000 IU Injection, powder, for solution Parenteral 2000 IU Injection, powder, for solution Parenteral 500 IU Powder, for solution Intravenous Injection, powder, for solution Intravenous Solution Parenteral 250 UI Injection, powder, for solution Parenteral Injection, powder, lyophilized, for solution Intravenous 500 iu/10ml Injection Intravenous Injection, powder, for solution Intravenous 1200 IU Injection, powder, for solution Parenteral 200 U.I. Injection, powder, for solution Parenteral 600 U.I. Injection, powder, for solution Parenteral 100 IU/ml Injection, powder, for solution Parenteral 50 IU/ml Injection, powder, for solution Parenteral 100 I.E./ml Injection, solution Intravenous 1000 iu/10ml Injection, solution Intravenous 500 iu/5ml Injection, powder, for solution Intravenous; Parenteral 3500 UI Injection, powder, for solution Parenteral 1200 I.E. Injection, powder, for solution Intravenous 120 IU/mL Injection, powder, for solution Parenteral 200 I.E. Injection, powder, for solution Parenteral 600 I.E. Powder, for solution Powder, for solution Intravenous 720 unit / 5 mL Injection, powder, for solution Intravenous Injection, powder, for solution Intravenous 1000 IU/10ML Powder, for solution Parenteral 200 UI/5ML Powder, for solution Parenteral 500 UI/10ML Injection, powder, lyophilized, for solution; kit Intravenous Powder, for solution Parenteral Solution Intravenous 500 UI Injection, powder, for suspension Parenteral 1000 IU Injection, powder, for solution Intravenous 1000 IU Injection, powder, for solution Intravenous 250 IU Injection, powder, for solution Intravenous 500 IU Injection, powder, lyophilized, for solution Intravenous 100 [iU]/1mL Kit Intravenous 1000 [iU]/10mL Kit Intravenous 500 [iU]/5mL Solution Parenteral 1000.0 UI Injection, powder, for solution Parenteral 50 I.E./ml Injection, powder, lyophilized, for solution Intravenous Kit; powder, for solution Intravenous Injection, powder, for solution Intravenous drip 520 IU/vial Injection Intravenous 1000 IU/10ml Injection Intravenous 1500 IU/10ml Injection Intravenous 500 IU/5ml Injection, powder, for solution Parenteral Injection, powder, for solution Intravenous 1000 UI Injection, powder, for solution Intravenous 2000 UI Injection, powder, for solution Intravenous 3000 UI Solution Parenteral 500.000 UI Injection, powder, for solution 50 iu/1vial Injection, powder, for solution Intravenous 500 iu/vial Injection, powder, lyophilized, for solution Intravenous 250 IU Solution Intravenous Injection, powder, for solution 600 iu/1vial Powder 100 iu/1vial - Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Liquid
- Experimental Properties
Property Value Source melting point (°C) 54 °C Link, R.P., Castellino, F.J. Arch. Biochem. Biophsy. 227:259-265 (1983) hydrophobicity -0.431 Not Available isoelectric point 5.20 Not Available
Targets
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Activator
- General Function
- Serine-type endopeptidase activity
- Specific Function
- Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
- Gene Name
- F10
- Uniprot ID
- P00742
- Uniprot Name
- Coagulation factor X
- Molecular Weight
- 54731.255 Da
References
- Worfolk LA, Robinson RA, Tracy PB: Factor Xa interacts with two sites on monocytes with different functional activities. Blood. 1992 Oct 15;80(8):1989-97. [Article]
- Jones KC, Mann KG: A model for the tissue factor pathway to thrombin. II. A mathematical simulation. J Biol Chem. 1994 Sep 16;269(37):23367-73. [Article]
- Ambrosini G, Plescia J, Chu KC, High KA, Altieri DC: Activation-dependent exposure of the inter-EGF sequence Leu83-Leu88 in factor Xa mediates ligand binding to effector cell protease receptor-1. J Biol Chem. 1997 Mar 28;272(13):8340-5. [Article]
- London FS, Walsh PN: Zymogen factor IX potentiates factor IXa-catalyzed factor X activation. Biochemistry. 2000 Aug 15;39(32):9850-8. [Article]
- Scandella DH: Properties of anti-factor VIII inhibitor antibodies in hemophilia A patients. Semin Thromb Hemost. 2000;26(2):137-42. [Article]
- Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [Article]
- Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Ligand
- General Function
- Serine-type endopeptidase activity
- Specific Function
- Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX.
- Gene Name
- F11
- Uniprot ID
- P03951
- Uniprot Name
- Coagulation factor XI
- Molecular Weight
- 70108.56 Da
References
- Sun MF, Zhao M, Gailani D: Identification of amino acids in the factor XI apple 3 domain required for activation of factor IX. J Biol Chem. 1999 Dec 17;274(51):36373-8. [Article]
- Gailani D, Ho D, Sun MF, Cheng Q, Walsh PN: Model for a factor IX activation complex on blood platelets: dimeric conformation of factor XIa is essential. Blood. 2001 May 15;97(10):3117-22. [Article]
- Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Ligand
- General Function
- Serine-type peptidase activity
- Specific Function
- Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, o...
- Gene Name
- F7
- Uniprot ID
- P08709
- Uniprot Name
- Coagulation factor VII
- Molecular Weight
- 51593.465 Da
References
- Baker DC, Robbe SL, Jacobson L, Manco-Johnson MJ, Holler L, Lefkowitz J: Hereditary deficiency of vitamin-K-dependent coagulation factors in Rambouillet sheep. Blood Coagul Fibrinolysis. 1999 Mar;10(2):75-80. [Article]
- Hertzberg MS, Facey SL, Hogg PJ: An Arg/Ser substitution in the second epidermal growth factor-like module of factor IX introduces an O-linked carbohydrate and markedly impairs activation by factor XIa and factor VIIa/Tissue factor and catalytic efficiency of factor IXa. Blood. 1999 Jul 1;94(1):156-63. [Article]
- Butenas S, van't Veer C, Mann KG: "Normal" thrombin generation. Blood. 1999 Oct 1;94(7):2169-78. [Article]
- Celie PH, Lenting PJ, Mertens K: Hydrophobic contact between the two epidermal growth factor-like domains of blood coagulation factor IX contributes to enzymatic activity. J Biol Chem. 2000 Jan 7;275(1):229-34. [Article]
- Shord SS, Lindley CM: Coagulation products and their uses. Am J Health Syst Pharm. 2000 Aug 1;57(15):1403-17; quiz 1418-20. [Article]
- Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Cofactor
- General Function
- Oxidoreductase activity
- Specific Function
- Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa.
- Gene Name
- F8
- Uniprot ID
- P00451
- Uniprot Name
- Coagulation factor VIII
- Molecular Weight
- 267007.42 Da
References
- Neels JG, Bovenschen N, van Zonneveld AJ, Lenting PJ: Interaction between factor VIII and LDL receptor-related protein. Modulation of coagulation? Trends Cardiovasc Med. 2000 Jan;10(1):8-14. [Article]
- Carr ME Jr, Martin EJ, Kuhn JG, Seremetis SV: Effects of recombinant factor VIIa on platelet function and clot structure in blood with deficient prothrombin conversion. Thromb Haemost. 2003 May;89(5):803-11. [Article]
- Federici AB: The factor VIII/von Willebrand factor complex: basic and clinical issues. Haematologica. 2003 Jun;88(6):EREP02. [Article]
- Kalashnikova LA, Berkovskii AL, Dobrynina LA, Sergeeva EV, Kozlov AA, Aleksandrova EN, Nasonov EL: [Clotting factor VIII in Sneddon syndrome]. Klin Med (Mosk). 2003;81(9):42-5. [Article]
- Johansen RF, Sorensen B, Ingerslev J: Acquired haemophilia: dynamic whole blood coagulation utilized to guide haemostatic therapy. Haemophilia. 2006 Mar;12(2):190-7. [Article]
- Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Thrombospondin receptor activity
- Specific Function
- Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostas...
- Gene Name
- F2
- Uniprot ID
- P00734
- Uniprot Name
- Prothrombin
- Molecular Weight
- 70036.295 Da
References
- Butenas S, van't Veer C, Mann KG: "Normal" thrombin generation. Blood. 1999 Oct 1;94(7):2169-78. [Article]
- Kohler M: Thrombogenicity of prothrombin complex concentrates. Thromb Res. 1999 Aug 15;95(4 Suppl 1):S13-7. [Article]
- Seitz R, Dodt J: Virus safety of prothrombin complex concentrates and factor IX concentrates. Thromb Res. 1999 Aug 15;95(4 Suppl 1):S19-23. [Article]
- Samis JA, Ramsey GD, Walker JB, Nesheim ME, Giles AR: Proteolytic processing of human coagulation factor IX by plasmin. Blood. 2000 Feb 1;95(3):943-51. [Article]
- Bauer KA, Humphries S, Smillie B, Li L, Cooper JA, Barzegar S, Rosenberg RD, Miller GJ: Prothrombin activation is increased among asymptomatic carriers of the prothrombin G20210A and factor V Arg506Gln mutations. Thromb Haemost. 2000 Sep;84(3):396-400. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Receptor activity
- Specific Function
- Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance...
- Gene Name
- LRP1
- Uniprot ID
- Q07954
- Uniprot Name
- Prolow-density lipoprotein receptor-related protein 1
- Molecular Weight
- 504601.695 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Rohlena J, Kolkman JA, Boertjes RC, Mertens K, Lenting PJ: Residues Phe342-Asn346 of activated coagulation factor IX contribute to the interaction with low density lipoprotein receptor-related protein. J Biol Chem. 2003 Mar 14;278(11):9394-401. Epub 2003 Jan 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Gamma-glutamyl carboxylase activity
- Specific Function
- Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vit...
- Gene Name
- GGCX
- Uniprot ID
- P38435
- Uniprot Name
- Vitamin K-dependent gamma-carboxylase
- Molecular Weight
- 87560.065 Da
References
- Lin PJ, Straight DL, Stafford DW: Binding of the factor IX gamma-carboxyglutamic acid domain to the vitamin K-dependent gamma-glutamyl carboxylase active site induces an allosteric effect that may ensure processive carboxylation and regulate the release of carboxylated product. J Biol Chem. 2004 Feb 20;279(8):6560-6. Epub 2003 Dec 2. [Article]
- Wu SM, Mutucumarana VP, Geromanos S, Stafford DW: The propeptide binding site of the bovine gamma-glutamyl carboxylase. J Biol Chem. 1997 May 2;272(18):11718-22. [Article]
- Rehemtulla A, Roth DA, Wasley LC, Kuliopulos A, Walsh CT, Furie B, Furie BC, Kaufman RJ: In vitro and in vivo functional characterization of bovine vitamin K-dependent gamma-carboxylase expressed in Chinese hamster ovary cells. Proc Natl Acad Sci U S A. 1993 May 15;90(10):4611-5. [Article]
- Stanley TB, Wu SM, Houben RJ, Mutucumarana VP, Stafford DW: Role of the propeptide and gamma-glutamic acid domain of factor IX for in vitro carboxylation by the vitamin K-dependent carboxylase. Biochemistry. 1998 Sep 22;37(38):13262-8. [Article]
- Stanley TB, Stafford DW, Olivera BM, Bandyopadhyay PK: Identification of a vitamin K-dependent carboxylase in the venom duct of a Conus snail. FEBS Lett. 1997 Apr 21;407(1):85-8. [Article]
Drug created at November 18, 2016 21:36 / Updated at February 20, 2024 23:54