Aprotinin

Aprotinin Basic information
Product Name:Aprotinin
Synonyms:TRYPSIN INHIBITOR, PANCREAS TYPE;TRYPSIN INHIBITOR (BASIC);TRYPSIN INHIBITOR, BOVINE LUNG;TRASYLOL;antikrein;antilysin;antilysine;aprotininfrombovinelung
CAS:9087-70-1
MF:C284H432N84O78R2S7
MW:6495.43988
EINECS:232-994-9
Product Categories:inhibitor;Affinity Chromatography;Protein Chromatography;Specialty Resins;ProteaseInhibitors
Mol File:9087-70-1.mol
Aprotinin Structure
Aprotinin Chemical Properties
Melting point >234oC (dec.)
storage temp. 2-8°C
solubility glycerol: soluble3mg/mL, clear, colorless (equilibration buffer containing 5% glycerol)
form lyophilized powder
color white
Water Solubility Freely soluble in water and in aqueous buffers of low ionic strength.
Merck 13,761
Stability:Stable. Incompatible with strong oxidizing agents.
Safety Information
Hazard Codes Xn,Xi
Risk Statements 42/43-36/37/38-20/21/22
Safety Statements 22-45-36/37-36-26
WGK Germany 1
RTECS YN5080000
10-21
HS Code 35040000
Hazardous Substances Data9087-70-1(Hazardous Substances Data)
ToxicityLD50 i.v. in mice: 2500000 kallikrein inhibitor units/kg (Trautschold)
MSDS Information
ProviderLanguage
Aprotinin English
SigmaAldrich English
Aprotinin Usage And Synthesis
DescriptionAprotinin 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.
Chemical Propertieswhite powder
OriginatorTrasylol,Bayer
UsesA 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.
UsesAprotinin is largely used as an inhibitor of trypsin.
Manufacturing Process1 kg of parotid of cattle, which were freed of fat and flesh are comminuted in a meat chopper and twice extracted with 5 L of acetone. The acetone was removed as far as possible by sucking off and the moist material is digested for 2.5 hours in 1.2 L of 1 N acetic acid and 2.8 L of 96% ethanol at 50°C. The filtrate containts about 230.000 inactivator units.
The alcoholic solution is concentrated to 1.2 L by evaporating in vacuo and shaken with an equal amount of ether. Dark coloring matters and residues of fat are thus dissolved. The aqueous phase is now mixed with acetone until a precipitate occurs and the dissolved in dilute acetic acid. The solution is brought to a weakly alkaline pH by addition of ammonia. It is then centrifuged and the inactivator is precipitated with five times the amount of ethanol. The yield amounts to about 180.000 kallikrein inactivator units in 0.4-0.5 g of substance.
Brand nameTrasylol (Bayer).
Therapeutic FunctionProteinase inhibitor
General DescriptionTrypsin inhibitor, pancreas type from bovine lung. It is known as Pancreatic trypsin inhibitor (BPTI). Aprotinin, also known as pancreatic trypsin inhibitor and trypsin-kallikrein inhibitor, is found to be expressed in lungs, spleen, liver, and pancreas. It is also found to be present in the free form in calf serum.
Biochem/physiol ActionsAprotinin is a competitive serine protease inhibitor that forms stable complexes with and blocks the active sites of enzyme. This binding is reversible, and most aprotinin-protease complexes will dissociate at extreme pH levels >10 or <3. Structurally, Aprotinin is a monomeric globular protein derived from bovine lung that consists of 58 amino acids, arranged in a single polypeptide chain with three crosslinking disulfide bridges.
Safety ProfileExperimental reproductive effects. When heated to decomposition it emits toxic fumes of NOx and SOx.
storageStore at +4°C
references1. henry da, carless pa, moxey aj, et al. anti-fibrinolytic use for minimising perioperative allogeneic blood transfusion. cochrane database syst rev 2007; 4: cd001886.2. levi m, cromheecke me, de jonge e, et al. pharmacological strategies to decrease excessive blood loss in cardiac surgery: a meta-analysis of clinically relevant endpoints. lancet 1999; 354: 1940-7.3. sedrakyan a, treasure t, elefteriades ja. effect of aprotinin on clinical outcomes in coronary artery bypass graft surgery: a systematic review and meta-analysis of randomized
Aprotinin Preparation Products And Raw materials
Raw materialsTrichloroacetic acid-->Ammonia-->Acetic acid-->Acetone
Aluminum acetylacetonate METHYL ISOCYANOACETATE N-BUTYLISOCYANIDE PHENYLSELENOL Tris(2,4-pentanedionato)chroMiuM(III) DICHLORO(ETHYLENEDIAMINE)PLATINUM(II) SALCOMINE 2,4-PENTANEDIONE, SILVER DERIVATIVE 1,1,3,3-TETRAMETHYLBUTYL ISOCYANIDE Tosylmethyl isocyanide COBALT(II) ACETYLACETONATE Cupric acetylacetonate Ethyl isocyanoacetate TERT-BUTYL ISOCYANIDE Ferric acetylacetonate COBALT ETHYLENE DIAMINE CHLORIDE Benzyl isocyanide TRIS(2,2,6,6-TETRAMETHYL-3,5-HEPTANEDIONATO)DYSPROSIUM(III)

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