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

Sequence

H-Pro-Asp-Phe-Cys-Leu-Glu-Pro-Pro-Tyr-Thr-Gly-Pro-Cys-Lys-Ala-Arg-Ile-Ile-Arg-Tyr-Phe-Tyr-Asn-Ala-Lys-Ala-Gly-Leu-Cys-Gln-Thr-Phe-Val-Tyr-Gly-Gly-Cys-Arg-Ala-Lys-Arg-Asn-Asn-Phe-Lys-Ser-Ala-Glu-Asp-Cys-Met-Arg-Thr-Cys-Gly-Gly-Ala-OH

Stability:

Stable. Incompatible with strong oxidizing agents.

InChIKey

RWLBZZCCAZDWSE-BNRYNCRGNA-N

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

F 

10-21

HS Code 

35040000

Hazardous Substances Data

9087-70-1(Hazardous Substances Data)

Toxicity

LD50 i.v. in mice: 2500000 kallikrein inhibitor units/kg (Trautschold)

MSDS

• Language:English Provider:Aprotinin
• Language:English Provider:SigmaAldrich

Aprotinin Usage And Synthesis

Description

Aprotinin is a reversible inhibitor of serine proteases such as trypsin (K_i = 0.06 pM), chymotrypsin (K_i = 9.5 nM), and kallikrein (K_i = 0.8 nM). It is a much weaker inhibitor of thrombin (K_i = 0.1-0.8 mM) and trypsinogen (K_i = 2 μM). Aprotinin also competitively inhibits nNOS and iNOS with K_i 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 Properties

white powder

Originator

Trasylol,Bayer

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.

Uses

Aprotinin is largely used as an inhibitor of trypsin.

Manufacturing Process

1 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 name

Trasylol (Bayer).

Therapeutic Function

Proteinase inhibitor

General Description

Trypsin 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 Actions

Aprotinin 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 Profile

Experimental reproductive effects. When heated to decomposition it emits toxic fumes of NOx and SOx.

storage

Store at +4°C

References

1. 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

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