Aprotinin, from bovine lung

Base Information

• Chemical Name: Aprotinin, from bovine lung
• CAS No.: 9087-70-1
• Molecular Formula: Unspecified
• Molecular Weight: 6511.44
• Hs Code.: 35040000
• European Community (EC) Number: 232-994-9
• Wikipedia: Aprotinin
• NCI Thesaurus Code: C47402
• RXCUI: 1056
• Mol file: 9087-70-1.mol

Synonyms:Antilysin;Aprotinin;Basic Pancreatic Trypsin Inhibitor;Bovine Kunitz Pancreatic Trypsin Inhibitor;Bovine Pancreatic Trypsin Inhibitor;BPTI, Basic Pancreatic Trypsin Inhibitor;Contrical;Contrykal;Dilmintal;Inactivator, Kallikrein-Trypsin;Iniprol;Kallikrein Trypsin Inactivator;Kallikrein-Trypsin Inactivator;Kontrikal;Kontrykal;Kunitz Pancreatic Trypsin Inhibitor;Pulmin;Traskolan;Trasylol;Trypsin Inhibitor, Basic, Pancreatic;Trypsin Inhibitor, Kunitz, Pancreatic;Zymofren

Chemical Property of Aprotinin, from bovine lung

Chemical Property:

• PSA: 0.00000
• LogP: 0.00000
• Storage Temp.: 2-8°C
• Solubility.: glycerol: soluble3mg/mL, clear, colorless (equilibration buffer
• Water Solubility.: Freely soluble in water and in aqueous buffers of low ionic strength.
• XLogP3: -25.4
• Hydrogen Bond Donor Count: 93
• Hydrogen Bond Acceptor Count: 97
• Rotatable Bond Count: 111
• Exact Mass: 6510.0514478
• Heavy Atom Count: 454
• Complexity: 16700

Purity/Quality:

98% ^*data from raw suppliers

Aprotinin ^*data from reagent suppliers

Safty Information:

• Pictogram(s): R42/43:
• Hazard Codes: Xn,Xi
• Statements: 42/43-36/37/38-20/21/22
• Safety Statements: 22-45-36/37-36-26

MSDS Files:

SDS file from LookChem

Total 1 MSDS from other Authors

Useful:

• Chemical Classes: Other Uses -> Biochemical Research
• Canonical SMILES: CCC(C)C1C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC2CSSCC3C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(CSSCC(C(=O)NC(C(=O)NC(C(=O)N4CCCC4C(=O)N5CCCC5C(=O)NC(C(=O)NC(C(=O)NCC(=O)N6CCCC6C(=O)NC(CSSCC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)N3)CC(=O)O)CCC(=O)O)C)CO)CCCCN)CC7=CC=CC=C7)CC(=O)N)CC(=O)N)CCCNC(=N)N)CCCCN)C)CCCNC(=N)N)NC(=O)CNC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC2=O)CCC(=O)N)C(C)O)CC8=CC=CC=C8)C(C)C)CC9=CC=C(C=C9)O)C(=O)NC(C(=O)NC(C(=O)NC(C(=O)N1)CCCNC(=N)N)C)CCCCN)C(C)O)CC1=CC=C(C=C1)O)CCC(=O)O)CC(C)C)NC(=O)C(CC1=CC=CC=C1)NC(=O)C(CC(=O)O)NC(=O)C1CCCN1C(=O)C(CCCNC(=N)N)N)C(=O)NCC(=O)NCC(=O)NC(C)C(=O)O)C(C)O)CCCNC(=N)N)CCSC)CC(C)C)C)CCCCN)C)CC(=O)N)CC1=CC=C(C=C1)O)CC1=CC=CC=C1)CC1=CC=C(C=C1)O)CCCNC(=N)N)C(C)CC
• Isomeric SMILES: CC[C@H](C)[C@H]1C(=O)N[C@@H](C(=O)N[C@@H](C(=O)N[C@@H](C(=O)N[C@H](C(=O)N[C@@H](C(=O)N[C@H](C(=O)N[C@@H](C(=O)N[C@H](C(=O)N[C@@H](C(=O)NCC(=O)N[C@@H](C(=O)N[C@@H]2CSSC[C@@H]3C(=O)N[C@H](C(=O)N[C@@H](C(=O)N[C@H](C(=O)N[C@@H](CSSC[C@H](C(=O)N[C@@H](C(=O)N[C@H](C(=O)N4CCC[C@@H]4C(=O)N5CCC[C@H]5C(=O)N[C@@H](C(=O)N[C@@H](C(=O)NCC(=O)N6CCC[C@H]6C(=O)N[C@H](CSSC[C@H](C(=O)N[C@H](C(=O)N[C@@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](C(=O)N[C@H](C(=O)N[C@@H](C(=O)N[C@H](C(=O)N[C@@H](C(=O)N[C@H](C(=O)N[C@@H](C(=O)N[C@H](C(=O)N3)CC(=O)O)CCC(=O)O)C)CO)CCCCN)CC7=CC=CC=C7)CC(=O)N)CC(=O)N)CCCNC(=N)N)CCCCN)C)CCCNC(=N)N)NC(=O)CNC(=O)CNC(=O)[C@@H](NC(=O)[C@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC2=O)CCC(=O)N)[C@@H](C)O)CC8=CC=CC=C8)C(C)C)CC9=CC=C(C=C9)O)C(=O)N[C@H](C(=O)N[C@@H](C(=O)N[C@H](C(=O)N1)CCCNC(=N)N)C)CCCCN)[C@H](C)O)CC1=CC=C(C=C1)O)CCC(=O)O)CC(C)C)NC(=O)[C@H](CC1=CC=CC=C1)NC(=O)[C@@H](CC(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](CCCNC(=N)N)N)C(=O)NCC(=O)NCC(=O)N[C@H](C)C(=O)O)[C@@H](C)O)CCCNC(=N)N)CCSC)CC(C)C)C)CCCCN)C)CC(=O)N)CC1=CC=C(C=C1)O)CC1=CC=CC=C1)CC1=CC=C(C=C1)O)CCCNC(=N)N)[C@H](C)CC
• Recent ClinicalTrials: An Open Non-comparative Study of the Efficacy and Safety of Aprotinin in Patients Hospitalized With COVID-19
• Recent EU Clinical Trials: Phase 3 randomized study to evaluate the safety and efficacy of aprotinin (Trasylol?) administered by inhalation nebulization in patients diagnosed with SARS-CoV-2 (COVID-19) with moderate severity compared to standard therapy.
• Description: Aprotinin is a reversible inhibitor of serine proteases such as trypsin (Ki = 0.06 pM), chymotrypsin (Ki = 9.5 nM), and kallikrein (Ki = 0.8 nM). It is a much weaker inhibitor of thrombin (Ki = 0.1-0.8 mM) and trypsinogen (Ki = 2 μM). Aprotinin also competitively inhibits nNOS and iNOS with Ki values of 50 and 78 μM, respectively. Aprotinin is widely used as a protein purification tool to prevent proteases present in tissue samples from degrading the protein of interest.
• Uses: A potent protease inhibitor.Aprotinin acts as a reversible serine protease blocking and a binding agent. It is widely employed as an inhibitor of trypsin. It is also used as a proteolytic inhibitor in radioimmunoassays of polypeptide hormones. It is involved in the purification of urokinase, trypsin, and chymotrypsin on immobilized aprotinin. Further, it is used in the quantification of kallikrein activity in mixtures of esterases and proteases. Aprotinin is largely used as an inhibitor of trypsin. Proteolytic inhibitor in radioimmunoassays of polypeptide hormones.
• Therapeutic Function: Proteinase inhibitor