Grundinformationen
- Standard-SMILES
O=C(O)C1CC(C2CCCCC2)CN1- InChIKey
XRZWVSXEDRYQGC-UHFFFAOYSA-N- Summenformel
- C11H19NO2
- Durchschnittliche Molmasse
- 197,27 g/mol
- Monoisotopische Masse
- 197,14157885
Überblick
Streptokinase, is a sterile, purified preparation of a bacterial protein elaborated by group C (beta) -hemolytic streptococci.
Namen und Bezeichner
- Bevorzugter Name
- Streptokinase
- IUPAC
- 4-cyclohexylpyrrolidine-2-carboxylic acid
- Lokaler Name
- Kinase (enzymaktivierend), Strepto-
- Englischer Name
- STREPTOKINASE
- Summenformel
- C11H19NO2
- Molmasse
- 197.27406
Namen und Synonyme
Weitere Namen anzeigen
Datenbank-Bezeichner
- CAS
1219214-76-2、9002-01-1- PubChem CID
- 9815560
- DTXSID
DTXSID00864144- ChEMBL
CHEMBL2108147- EC Number
- 232-647-1
Eigenschaften
Berechnete Struktureigenschaften
- XLogP
- 0,3
- Polarare Oberfläche (TPSA)
- 49,3 Ų
- H-Brücken-Donoren
- 2
- H-Brücken-Akzeptoren
- 3
- Frei drehbare Bindungen
- 2
- Schwere Atome
- 14
- Formalladung
- 0
- Komplexität
- 211
Experimentelle und physikochemische Eigenschaften
Physikochemische Eigenschaften
- storage temp.
- -20 °C · -20°C
- Aggregatzustand
- lyophilized powder
- Farbe
- White to off-white
- Biologische Quelle
- human
- Merck
- 13 · 13,8903
- Specific Activity
- 2 · ≥2,000units/mg solid
- InChI
- 1S/C11H19NO2/c13-11(14)10-6-9(7-12-10)8-4-2-1-3-5-8/h8-10,12H,1-7H2,(H,13,14)
- InChIKey
- XRZWVSXEDRYQGC-UHFFFAOYSA-N
- SMILES
- N1C(CC(C1)C2CCCCC2)C(=O)O
Sicherheit und Regulatorisches
GHS-Klassifizierung
GHS Classification
Danger
H334 (100%): May cause allergy or asthma symptoms or breathing difficulties if inhaled [Danger Sensitization, respiratory]
P233, P260, P271, P284, P304+P340, P342+P316, P403, and P501 (click each P-code to see the statement)
Aggregated GHS information provided per 131 reports by companies from 1 notifications to the ECHA C&L Inventory.
Gefahrenhinweise
Toxikologische Informationen
Adverse Effects
Allergic reactions and bleeding are common adverse events related to streptokinase. The GISSI study demonstrated a 3.4% incidence of minor bleeding. The ISSI-2 study demonstrates a 0.4% incidence of significant bleeding. Patients may experience transient bradycardia or hypotension, with an incidence of 10%. Streptokinase is derived from bacterial proteins and thus can result in allergic reactions. Allergic reactions have been noted in up to 4.4% of patients and may present with fever, shivering, or rash. In rare cases, anaphylaxis may occur, which appears to be IgE mediated. Patients who develop anaphylactic signs and symptoms should promptly discontinue treatment and receive epinephrine.
Toxicity Summary
Streptokinase can precipitate an allergic reaction. Symptoms include fever, shivering, and rash. Patients in rare instances have developed nonfatal anaphylactic reactions. In cases of anaphylaxis, patients should be administered epinephrine immediately and discontinue streptokinase therapy. The toxicity of streptokinase is believed to be because it is a polypeptide derivative of beta-hemolytic streptococci bacteria.
Plasminogen is an inactive molecule that becomes activated to plasmin when the Arg/Val bond is cleaved. Plasmin breaks down fibrin clots created by the blood clotting cascade. Streptokinase forms a highly specific 1:1 enzymatic complex with plasminogen which converts inactive plasminogen molecules into active plasmin. Plasmin degrades fibrin clots as well as fibrinogen and other plasma proteins. This in turn leads to the degradation of blood clots.
Drug Induced Liver Injury
Drug-Induced Liver Injury Severity and Toxicity (DILIst)
STREPTOKINASE
DILI Positive
Intracoronary; Intravenous
DOI:10.1016/j.drudis.2019.09.022
Sicherheitsdaten
- F
- 10-21
- wgk
- 3
- hs_code
- 3504009000
- RTECS-Nr.
- OB8880000
- risk_code
- 36/37/38
- Toxizität
- LD50 oral in mouse: > 10gm/kg
- hazard_code
- B,Xi
- safety_code
- 22-24/25-36-26
- Speicherklasse
- 11 - Combustible Solids
Chemie und Industrie
Pharmakologische Informationen
ATC Code
B - Blood and blood forming organs
QB - Blood and blood forming organs
B01AD01
Pharmacodynamics
Streptokinase creates an active complex which promotes the cleavage of the Arg/Val bond in plasminogen to form the proteolytic enzyme plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction.
Mechanism of Action
Plasminogen is an inactive molecule that becomes activated to plasmin when the Arg/Val bond is cleaved. Plasmin breaks down fibrin clots created by the blood clotting cascade. Streptokinase forms a highly specific 1:1 enzymatic complex with plasminogen which converts inactive plasminogen molecules into active plasmin. Plasmin degrades fibrin clots as well as fibrinogen and other plasma proteins. This in turn leads to the degradation of blood clots.
Metabolism/Metabolites
Free toxin may be removed by opsonization via the reticuloendothelial system (primarily the liver and kidneys) or it may be degraded through cellular internalization via the lysosomes. Lysosomes are membrane-enclosed organelles that contain an array of digestive enzymes, including several proteases.
Verwendung und Herstellung
Anwendungen
BeschreibungStreptokinase is a protein produced by certain strains of hemolytic group C streptococcus, and it was the first clinically useful fibrinolytic. Unlike other plasminogen activators, streptokinase is not an enzyme and cannot break any bonds in a plasminogen molecule by itself. It forms an equimolecular compound with plasminogen, thus forming a streptokinase–plasminogen complex. In the plasminogenic region of the resulting complex, certain conformational changes lead to a break in a few peptide bonds, and transformation of this complex into a streptokinase–plasmin complex, or free plasmin, which also decomposes fibrin.
VerwendenThis drug has a half-life in the plasma of 15–30 min, and is used intravenously to treat patients with severe, massive pulmonary embolism and thrombus of the veins; it is also used during myocardial infarctions. Recently, a number of streptokinase derivatives have been proposed, in particular acetylated derivatives, which are developed for use as fibrinolytics.
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