Product Information
Registration Status: ActiveSIN14719P
ARTISS SOLUTIONS FOR SEALANT, DEEP FROZEN is approved to be sold in Singapore with effective from 2015-06-01. It is marketed by BAXTER HEALTHCARE (ASIA) PTE LTD, with the registration number of SIN14719P.
This product contains Aprotinin 2250 3750 KIU/ml,Calcium Chloride 36 44 mcmol/ml,Human Fibrinogen 72 110mg/ml, and Human Thrombin 3.2 5.0 IU/ml in the form of SOLUTION. It is approved for TOPICAL use.
This product is manufactured by BAXTER AG (Site: Industriestrasse 72)
BAXTER AG (Site: Lange Allee 24B)
BAXTER AG (Site: Lange Allee 24A) (Primary in AUSTRIA.
It is a Prescription Only Medicine that can only be obtained from a doctor or a dentist, or a pharmacist with a prescription from a Singapore-registered doctor or dentist.
Product Reference
Important Note: For generic product, the SPC/PIL provided may not be brand specific.
{{/items}} {{^items}}Description
Aprotinin, also known as bovine pancreatic trypsin inhibitor, BPTI (Trasylol, Bayer) is a protein, that is used as medication administered by injection to reduce bleeding during complex surgery, such as heart and liver surgery. Its main effect is the slowing down of fibrinolysis, the process that leads to the breakdown of blood clots. The aim in its use is to decrease the need for blood transfusions during surgery, as well as end-organ damage due to hypotension (low blood pressure) as a result of marked blood loss. The drug was temporarily withdrawn worldwide in 2007 after studies suggested that its use increased the risk of complications or death; after this was confirmed by follow-up studies, Trasylol was entirely and permanently withdrawn in May 2008, except - at least for the time being - for very restricted research use.
Indication
For prophylactic use to reduce perioperative blood loss and the need for blood transfusion in patients undergoing cardiopulmonary bypass in the course of coronary artery bypass graft surgery who are at an increased risk for blood loss and blood transfusion.
Mechanism of Action
Aprotinin inhibits several serine proteases, specifically trypsin, chymotrypsin and plasmin at a concentration of about 125,000 IU/ml, and kallikrein at 300,000 IU/ml. Its action on kallikrein leads to the inhibition of the formation of factor XIIa. As a result, both the intrinsic pathway of coagulation and fibrinolysis are inhibited. Its action on plasmin independently slows fibrinolysis.
Pharmacokinetics
- Absorption
- 100% (IV)
- Distribution
- Metabolism
- Aprotinin is slowly degraded by lysosomal enzymes.
- Elimination
Active Ingredient/Synonyms
Aprotinin (bovine) | Aprotinin Biosynthetic | Aprotinin Bovine | Aprotinin Concentrated Solution | Bovine Aprotinin | Bovine Pancreatic Trypsin Inhibitor | BPTI | Fibrinolysis Inhibitor | Trypsin Inhibitor, Pancreatic Basic | Aprotinin |
Source of information: Drugbank (External Link). Last updated on: 3rd July 18. *Trade Name used in the content below may not be the same as the HSA-registered product.
Description
Calcium chloride is an ionic compound of calcium and chlorine. It is highly soluble in water and it is deliquescent. It is a salt that is solid at room temperature, and it behaves as a typical ionic halide. It has several common applications such as brine for refrigeration plants, ice and dust control on roads, and in cement. It can be produced directly from limestone, but large amounts are also produced as a by-product of the Solvay process. Because of its hygroscopic nature, it must be kept in tightly-sealed containers.
Indication
For the treatment of hypocalcemia in those conditions requiring a prompt increase in blood plasma calcium levels, for the treatment of magnesium intoxication due to overdosage of magnesium sulfate, and used to combat the deleterious effects of hyperkalemia as measured by electrocardiographic (ECG), pending correction of the increased potassium level in the extracellular fluid.
Mechanism of Action
Calcium chloride in water dissociates to provide calcium (Ca2+) and chloride (Cl-) ions. They are normal constituents of the body fluids and are dependent on various physiological mechanisms for maintenance of balance between intake and output. For hyperkalemia, the influx of calcium helps restore the normal gradient between threshold potential and resting membrane potential.
Toxicity
Too rapid injection may produce lowering of blood pressure and cardiac syncope. Persistent hypercalcemia from overdosage of calcium is unlikely because of rapid excretion.
Active Ingredient/Synonyms
Calcium chloride anhydrous | Calcium chloride, anhydrous | calcium(2+) chloride | Calcium Chloride |
Source of information: Drugbank (External Link). Last updated on: 3rd July 18. *Trade Name used in the content below may not be the same as the HSA-registered product.
Description
Fibrinogen concentrate (human) is a hematological agent. It works by replacing a certain protein in the blood that helps with blood clotting. Fibrinogen (factor I) is a soluble plasma glycoprotein with a molecular weight of about 340 kDa. It is a physiological substrate for three enzymes: plasmin, factor XIIIa and thrombin. it is indicated for the treatment of acute bleeding episodes in patients with congenital fibrinogen deficiency, including afibrinogenemia and hypofibrinogenemia.
Indication
For the treatment of acute bleeding episodes in patients with congenital fibrinogen deficiency, including afibrinogenemia and hypofibrinogenemia.
Mechanism of Action
Fibrinogen (factor I) is a soluble plasma glycoprotein with a molecular weight of about 340 kDa. The native molecule is a dimer and consists of three pairs of polypeptide chains (Aα, Bβ and γ). Fibrinogen is a physiological substrate of three enzymes: thrombin, factor XIIIa, and plasmin. During the coagulation process, thrombin cleaves the Aα and Bβ chains releasing fibrinopeptides A and B (FPA and FPB, respectively). FPA is separated rapidly and the remaining molecule is a soluble fibrin monomer (fibrin I). The slower removal of FPB results in formation of fibrin II that is capable of polymerization that occurs by aggregation of fibrin monomers. The resulting fibrin is stabilized in the presence of calcium ions and by activated factor XIII, which acts as a transglutaminase. Factor XIIIa-induced cross-linking of fibrin polymers renders the fibrin clot more elastic and more resistant to fibrinolysis. Cross-linked fibrin is the end result of the coagulation cascade, and provides tensile strength to a primary hemostatic platelet plug and structure to the vessel wall.
Pharmacokinetics
- Absorption
- Cmax is 140 mg/dL
- Distribution
- Mean volume of distribution is 52.7 mL/kg.
- Metabolism
- Elimination
Clearance
0.59 mL/h/kg
Active Ingredient/Synonyms
Coagulation Factor I | Factor I (fibrinogen) | Factor I human | Fibrinogen | Fibrinogen (human) | Fibrinogen Concentrate (Human) | Fibrinogen concentrate human | Fibrinogen human | Fibrinogen human plasma-derived | Fibrinogen, human | Human fibrinogen | Fibrinogen Human |
Source of information: Drugbank (External Link). Last updated on: 3rd July 18. *Trade Name used in the content below may not be the same as the HSA-registered product.
Description
Human Thrombin is a sterile solution, pH 6.8-7.2, containing highly purified human thrombin for the activation of clotting. Thrombin is a highly specific serine protease encoded by the F2 gene that transforms soluble fibrinogen into insoluble fibrin. This transformation mimics the final coagulation cascade step which involves the clotting mass that adheres to the wound surface and achieves hemostasis and sealing of open tissues. In particular, while human thrombin products are made from pooled human source plasma, recombinant thrombin is a human coagulation protein produced via recombinant DNA technology from a genetically modified Chinese hamster ovary cell line [FDA Label]. Furthermore, human thrombin is manufactured by chromatographic purification of prothrombin from cryo-poor plasma followed by activation with calcium chloride [FDA Label].
Indication
Human thrombin is indicated as an aid to hemostasis whenever oozing blood and minor bleeding from capillaries and small venules are accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical [FDA Label].
Mechanism of Action
Human thrombin (coagulation factor IIa) is a highly specific protease that transforms plasma fibrinogen into fibrin which, in the presence of clotting factor XIII in the patient's plasma, is cross-linked to form a stable clot [FDA Label]. When applied to a surgical wound where bleeding is present, thrombin activates fibrinogen in the patient's plasma to form fibrin, which results in clot formation and hemostasis [FDA Label]. The fibrin clot is stabilized by cross-linking occurring as a result of activation of the patient's endogenous factor XIII, which requires the presence of calcium [FDA Label]. Human thrombin does not require any intermediate physiological agent because it naturally clots the fibrinogen of the blood directly [FDA Label]. Any failure to clot blood occurs in the rare case where the primary clotting defect is the absence of fibrinogen itself [FDA Label]. The speed with which human thrombin clots blood is dependent upon the concentration of both the human thrombin used and fibrinogen present [FDA Label].
Pharmacokinetics
- Absorption
- Due to the nature of the product, which is intended for topical application to the surface of the tissue at the surgical site, pharmacokinetic studies were not conducted [FDA Label]. Particularly because the agent is topical, systemic absorption is expected to be small [A32427].
- Distribution
- Due to the nature of the product, which is intended for topical application to the surface of the tissue at the surgical site, pharmacokinetic studies were not conducted [FDA Label]. Precisely because human thrombin is applied only topically, systemic exposure or distribution to other organs and tissues is not expected [A32427].
- Metabolism
- Due to the nature of the product, which is intended for topical application to the surface of the tissue at the surgical site, pharmacokinetic studies were not conducted [FDA Label]. Nevertheless, commercial human thrombin products are expected to be metabolized in the same way as endogenous thrombin is. Endogenous thrombin does not circulate in the blood as a free, active molecule for very long [L2079]. After performing its function it is rapidly inactivated after formation of complexes with various circulating endogenous plasma inhibitors (like antithrombin III) [L2079]. This rapid inactivation prevents the active agent from diffusing into the general circulation. The complexes formed are then generally cleared and eliminated by the liver [L2079].
- Elimination
Clearance
Due to the nature of the product, which is intended for topical application to the surface of the tissue at the surgical site, pharmacokinetic studies were not conducted [FDA Label]. Regardless, commercial human thrombin, like endogenous thrombin, is generally rapidly neutralized by naturally circulating plasma inhibitors limiting its duration of action and preventing the active form from diffusing into the general circulation [L2079].
Toxicity
No cases of overdose have been reported at this time [FDA Label]. The LD50 value for the mouse model is calculated to be approximately 3 gm/kg [MSDS].
Active Ingredient/Synonyms
Thrombin (human) | Thrombin human | Thrombin Human Plasma-derived | Human Thrombin |
Source of information: Drugbank (External Link). Last updated on: 3rd July 18. *Trade Name used in the content below may not be the same as the HSA-registered product.