BIOMAT Database Logo BIOMAT Database Logo

Reduction of factor VIII and other coagulation factors by the thioredoxin system. 1979

G Savidge, and G Carlebjörk, and B Thorell, and B Hessel, and A Holmgren, and B Blombäck

UI MeSH Term Description Entries
D007611 Aprotinin A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995) BPTI, Basic Pancreatic Trypsin Inhibitor,Basic Pancreatic Trypsin Inhibitor,Bovine Kunitz Pancreatic Trypsin Inhibitor,Kallikrein-Trypsin Inactivator,Kunitz Pancreatic Trypsin Inhibitor,Trypsin Inhibitor, Basic, Pancreatic,Trypsin Inhibitor, Kunitz, Pancreatic,Antilysin,Bovine Pancreatic Trypsin Inhibitor,Contrical,Contrykal,Dilmintal,Iniprol,Kontrikal,Kontrykal,Pulmin,Traskolan,Trasylol,Zymofren,Inactivator, Kallikrein-Trypsin,Kallikrein Trypsin Inactivator
D008297 Male Males
D009247 NADH, NADPH Oxidoreductases A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6. Oxidoreductases, NADH, NADPH,NADPH Oxidoreductases NADH,Oxidoreductases NADH, NADPH
D010949 Plasma The residual portion of BLOOD that is left after removal of BLOOD CELLS by CENTRIFUGATION without prior BLOOD COAGULATION. Blood Plasma,Fresh Frozen Plasma,Blood Plasmas,Fresh Frozen Plasmas,Frozen Plasma, Fresh,Frozen Plasmas, Fresh,Plasma, Blood,Plasma, Fresh Frozen,Plasmas,Plasmas, Blood,Plasmas, Fresh Frozen
D001779 Blood Coagulation Factors Endogenous substances, usually proteins, that are involved in the blood coagulation process. Clotting Factor,Coagulation Factors,Blood Coagulation Factor,Clotting Factors,Coagulation Factor,Coagulation Factor, Blood,Coagulation Factors, Blood,Factor, Coagulation,Factors, Coagulation,Factor, Blood Coagulation,Factor, Clotting,Factors, Blood Coagulation,Factors, Clotting
D002850 Chromatography, Gel Chromatography on non-ionic gels without regard to the mechanism of solute discrimination. Chromatography, Exclusion,Chromatography, Gel Permeation,Chromatography, Molecular Sieve,Gel Filtration,Gel Filtration Chromatography,Chromatography, Size Exclusion,Exclusion Chromatography,Gel Chromatography,Gel Permeation Chromatography,Molecular Sieve Chromatography,Chromatography, Gel Filtration,Exclusion Chromatography, Size,Filtration Chromatography, Gel,Filtration, Gel,Sieve Chromatography, Molecular,Size Exclusion Chromatography
D005164 Factor IX Storage-stable blood coagulation factor acting in the intrinsic pathway of blood coagulation. Its activated form, IXa, forms a complex with factor VIII and calcium on platelet factor 3 to activate factor X to Xa. Deficiency of factor IX results in HEMOPHILIA B (Christmas Disease). Autoprothrombin II,Christmas Factor,Coagulation Factor IX,Plasma Thromboplastin Component,Blood Coagulation Factor IX,Factor 9,Factor IX Complex,Factor IX Fraction,Factor Nine,Factor IX, Coagulation
D005165 Factor V Heat- and storage-labile plasma glycoprotein which accelerates the conversion of prothrombin to thrombin in blood coagulation. Factor V accomplishes this by forming a complex with factor Xa, phospholipid, and calcium (prothrombinase complex). Deficiency of factor V leads to Owren's disease. Coagulation Factor V,Proaccelerin,AC Globulin,Blood Coagulation Factor V,Factor 5,Factor Five,Factor Pi,Factor V, Coagulation
D005169 Factor VIII Factor VIII of blood coagulation. Antihemophilic factor that is part of the factor VIII/von Willebrand factor complex. Factor VIII is produced in the liver and acts in the intrinsic pathway of blood coagulation. It serves as a cofactor in factor X activation and this action is markedly enhanced by small amounts of thrombin. Coagulation Factor VIII,Factor VIII Clotting Antigen,Factor VIII Coagulant Antigen,Factor VIII Procoagulant Activity,Thromboplastinogen,Blood Coagulation Factor VIII,F VIII-C,Factor 8,Factor 8 C,Factor Eight,Factor VIIIC,Hyate-C,Hyatt-C,F VIII C,Hyate C,HyateC,Hyatt C,HyattC
D005170 Factor X Storage-stable glycoprotein blood coagulation factor that can be activated to factor Xa by both the intrinsic and extrinsic pathways. A deficiency of factor X, sometimes called Stuart-Prower factor deficiency, may lead to a systemic coagulation disorder. Autoprothrombin III,Coagulation Factor X,Stuart Factor,Stuart-Prower Factor,Blood Coagulation Factor X,Factor 10,Factor Ten,Stuart Prower Factor,Factor X, Coagulation

Related Publications

G Savidge, and G Carlebjörk, and B Thorell, and B Hessel, and A Holmgren, and B Blombäck
Synthesis of procoagulant factor VIII, factor VIII related antigen and other coagulation factors by the isolated perfused rat liver.
April 1979, British journal of haematology,
G Savidge, and G Carlebjörk, and B Thorell, and B Hessel, and A Holmgren, and B Blombäck
The effect of reducing agents on factor VIII and other coagulation factors.
June 1978, Thrombosis research,
G Savidge, and G Carlebjörk, and B Thorell, and B Hessel, and A Holmgren, and B Blombäck
Structure-function relationships of human factor VIII complex studied by thioredoxin dependent disulfide reduction.
September 1984, Thrombosis research,
G Savidge, and G Carlebjörk, and B Thorell, and B Hessel, and A Holmgren, and B Blombäck
Pathogenic antibodies to coagulation factors. Part one: factor VIII and factor IX.
July 2004, Journal of thrombosis and haemostasis : JTH,
G Savidge, and G Carlebjörk, and B Thorell, and B Hessel, and A Holmgren, and B Blombäck
Coagulation factor VIII concentrates and the marketplace.
June 1988, Lancet (London, England),
G Savidge, and G Carlebjörk, and B Thorell, and B Hessel, and A Holmgren, and B Blombäck
Coagulation factor VIII concentrates and the marketplace.
July 1988, Lancet (London, England),
G Savidge, and G Carlebjörk, and B Thorell, and B Hessel, and A Holmgren, and B Blombäck
Reduction of purothionin by the wheat seed thioredoxin system.
October 1987, Plant physiology,
G Savidge, and G Carlebjörk, and B Thorell, and B Hessel, and A Holmgren, and B Blombäck
Blood coagulation factor VIII D1241E polymorphism leads to a weak malectin interaction and reduction of factor VIII posttranslational modification and secretion.
December 2020, Experimental cell research,
G Savidge, and G Carlebjörk, and B Thorell, and B Hessel, and A Holmgren, and B Blombäck
Coagulation factor VIII: structure and stability.
June 2003, International journal of pharmaceutics,
G Savidge, and G Carlebjörk, and B Thorell, and B Hessel, and A Holmgren, and B Blombäck
[Autoantibodies against coagulation factor VIII].
October 1998, Ugeskrift for laeger,
Copied contents to your clipboard!