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A1153 Sigma

Aprotinin from bovine lung

lyophilized powder, 3-8 TIU/mg solid

Synonym: Trasylol, Trypsin inhibitor (basic)

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Description

Frequently Asked Questions

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Application

Aprotinin is largely used as an inhibitor of trypsin.

Preparation Note

This product is a lyophilized powder with activity of 3-8 TIU/mg of solid powder. Aprotinin is freely soluble in water (>10 mg/mL) and in aqueous buffers of low ionic strengths. Dilute solutions tend to be less stable than concentrated ones, though solution stability also depends on pH. Aprotinin is relatively stable against denaturation - only thermolysin has been found capable of degrading it at 60-80°C. Sterilizaiton of Aprotinin can be achieved through filtration by a 0.2 μm filter.

Unit Definition

One Trypsin Inhibitor Unit (TIU) will decrease the activity of two trypsin units by 50%, where one trypsin unit will hydrolyze 1.0 μmole of Nalpha-benzoyl-DL-arginine p-nitroanilide per minute at pH 7.8 and 25°C. Another commonly used unit is the KIU, with 1 TIU = 1,300 KIU.

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.

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Aprotinin from bovine lung

lyophilized powder, 3-7 TIU/mg solid

Aprotinin from bovine lung

lyophilized powder, 3-8 TIU/mg solid, BioReagent, suitable for cell culture

Safety & Documentation

Safety Information

WGK Germany 
1
RTECS 
YN5080000

Protocols & Articles

Protocols

Enzymatic Assay of Aprotinin

2. SCOPE The scope of this procedure is all products that have a specification for Aprotinin activity.
Keywords: Enzymology, Extinction coefficient

Peer-Reviewed Papers

References

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Aprotinin in perspective Aprotinin in perspective Ann. Thorac. Surg. 55(4), 1033-1041, (1993)

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Aprotinin in cardiac surgery: a review of conventional and novel mechanisms of action McEvoy, M.D., et al. Anesth. Analg. 105, 949-962, (2007)

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Trautschold, I., et al. Biochem. Pharmacol. 16, 59, (1967)

Review: Biochemistry of aprotinin and aprotinin-like inhibitors. Gebhard, W. Res. Monogr. Cell Tissue Physiol. 12, 375, (1986)

Development Of A Drug Screening Platform Based On Engineered Heart Tissue. Hansen, A., et al. Circ. Res. 107, 35-44, (2010)

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Preparation of extracts from higher eukaryotes. Dignam, J.D Meth. Enzymol. 182, 194-203, (1990)

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Maintaining protein stability. Deutscher, M.P Meth. Enzymol. 182, 83-89, (1990)

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Antimicrobial Activity Of A Halocidin-derived Peptide Resistant To Attacks By Proteases. Shin, Y.P., et al. Anticancer Res. 54, 2855-66, (2010)

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Analysis Of Histones And Chromatin In Xenopus Laevis Egg And Oocyte Extracts Banaszynski, L.A., et al. Methods 51, 40247, (2010)

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Biochemical Characterization Of Native Usher Protein Complexes From A Vesicular Subfraction Of Tracheal Epithelial Cells. Zallocchi, M., et al. Biochem. Pharmacol. 49, 1236-47, (2010)

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RaPID: An Aptamer-based MRNA Affinity Purification Technique For The Identification Of RNA And Protein Factors Present In Ribonucleoprotein Complexes. Slobodin, B., and Gerst, J.E. Methods Mol. Biol. 714, 387-406, (2011)

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Tranexamic acid concentrations associated with human seizures inhibit glycine receptors. Lecker I, Wang DS, Romaschin AD, et al. J. Clin. Invest. 122(12), 4654-66, (2012)

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Structure and function of invertebrate Kunitz serine protease inhibitors. Ranasinghe S and McManus DP Dev. Comp. Immunol. 39(3), 219-27, (2013)

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Antifibrinolytics attenuate inflammatory gene expression after cardiac surgery. Later AF, Sitniakowsky LS, van Hilten JA, et al. J. Thorac. Cardiovasc. Surg. 145(6), 1611-6, 1616.e1-4, (2013)

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The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake. Millers EK, Johnson LA, Birrell GW, et al. PLoS ONE 8(1), e54104, (2013)

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The current place of aprotinin in the management of bleeding. Royston D Anaesthesia 70 Suppl 1, 46-9, e17, (2015)

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Regulatory decisions pertaining to aprotinin may be putting patients at risk. Hébert PC, Fergusson DA, Hutton B, et al. CMAJ 186(18), 1379-86, (2014)

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Antifibrinolytic drugs for acute traumatic injury. Roberts I, Shakur H, Ker K, et al. Cochrane Database Syst. Rev. 12, CD004896, (2012)

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Functional characterization of a slow and tight-binding inhibitor of plasmin isolated from Russell's viper venom. Cheng AC and Tsai IH Biochim. Biophys. Acta 1840(1), 153-9, (2014)

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Entropy-enthalpy transduction caused by conformational shifts can obscure the forces driving protein-ligand binding. Fenley AT, Muddana HS, and Gilson MK Proc. Natl. Acad. Sci. U. S. A. 109(49), 20006-11, (2012)

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Antifibrinolytic agents in current anaesthetic practice. Ortmann E, Besser MW, and Klein AA Br. J. Anaesth. 111(4), 549-63, (2013)

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A spider-derived Kunitz-type serine protease inhibitor that acts as a plasmin inhibitor and an elastase inhibitor. Wan H, Lee KS, Kim BY, et al. PLoS ONE 8(1), e53343, (2013)

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Age-dependent neonatal intracerebral hemorrhage in plasminogen activator inhibitor 1 knockout mice. Leroux P, Omouendze PL, Roy V, et al. J. Neuropathol. Exp. Neurol. 73(5), 387-402, (2014)

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Replacement of aprotinin by ε-aminocaproic acid in infants undergoing cardiac surgery: consequences for blood loss and outcome. Martin K, Gertler R, MacGuill M, et al. Br. J. Anaesth. 110(4), 615-21, (2013)

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Structural characterization of Spinacia oleracea trypsin inhibitor III (SOTI-III). Glotzbach B, Schmelz S, Reinwarth M, et al. Acta Crystallogr. D Biol. Crystallogr. 69(Pt 1), 114-20, (2013)

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Neutron and X-ray crystallographic analysis of Achromobacter protease I at pD 8.0: protonation states and hydration structure in the free-form. Ohnishi Y, Yamada T, Kurihara K, et al. Biochim. Biophys. Acta 1834(8), 1642-7, (2013)

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Comparison of complexes formed by a crustacean and a vertebrate trypsin with bovine pancreatic trypsin inhibitor - the key to achieving extreme stability? Molnár T, Vörös J, Szeder B, et al. FEBS J. 280(22), 5750-63, (2013)

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Functional microRNA library screening identifies the hypoxamir miR-24 as a potent regulator of smooth muscle cell proliferation and vascularization. Fiedler J, Stöhr A, Gupta SK, et al. Antioxid. Redox Signal. 21(8), 1167-76, (2014)

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Oxidative folding of peptides with cystine-knot architectures: kinetic studies and optimization of folding conditions. Reinwarth M, Glotzbach B, Tomaszowski M, et al. ChemBioChem. 14(1), 137-46, (2013)

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Matching on provider is risky. Walker AM J. Clin. Epidemiol. 66(8 Suppl), S65-8, (2013)

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Aprotinin may increase mortality in low and intermediate risk but not in high risk cardiac surgical patients compared to tranexamic acid and ε-aminocaproic acid -- a meta-analysis of randomised and observational trials of over 30.000 patients. Meybohm P, Herrmann E, Nierhoff J, et al. PLoS ONE 8(3), e58009, (2013)

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A comparative study of the immune modulating properties of antifibrinolytics in cardiac surgery. Later AF, Bruggemans EF, Romijn FP, et al. Cytokine 61(2), 438-44, (2013)

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Ring flips revisited: (13)C relaxation dispersion measurements of aromatic side chain dynamics and activation barriers in basic pancreatic trypsin inhibitor. Weininger U, Modig K, and Akke M Biochemistry 53(28), 4519-25, (2014)

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Cell-free synthesis system suitable for disulfide-containing proteins. Matsuda T, Watanabe S, and Kigawa T Biochem. Biophys. Res. Commun. 431(2), 296-301, (2013)

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Gene expression of tissue-specific molecules in ex vivo Dermacentor variabilis (Acari: Ixodidae) during rickettsial exposure. Sunyakumthorn P, Petchampai N, Grasperge BJ, et al. J. Med. Entomol. 50(5), 1089-96, (2013)

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Coronary artery bypass grafting after aprotinin: are we doing better? Beckerman Z, Shopen Y, Alon H, et al. J. Thorac. Cardiovasc. Surg. 145(1), 243-8, (2013)

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Protein conformational space populated in solution probed with aromatic residual dipolar (13) C-(1) H couplings. Sathyamoorthy B, Singarapu KK, Garcia AE, et al. ChemBioChem. 14(6), 684-8, (2013)

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Effect of pH and temperature on stability and kinetics of novel extracellular serine alkaline protease (70 kDa). Bhunia B, Basak B, Mandal T, et al. Int. J. Biol. Macromol. 54, 1-8, (2013)

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The risks associated with aprotinin use: a retrospective study of cardiac cases in Nova Scotia. Riddell RE, Buth KJ, and Sullivan JA Can. J. Anaesth. 60(1), 16-23, (2013)

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Influence of different storage conditions and anticoagulants on the measurement of total and acylated ghrelin in dogs: a preliminary study. Tvarijonaviciute A, Martínez-Subiela S, and Ceron JJ Vet. Rec. 172(11), 289, (2013)

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Analysis of protein aggregation kinetics using short amino acid peptide tags. Khan MA, Islam MM, and Kuroda Y Biochim. Biophys. Acta 1834(10), 2107-15, (2013)

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Retrospective cohort analysis of a single dose of aprotinin use in children undergoing cardiac surgery: a single-center experience. Fan Y, Lin R, Yang L, et al. Paediatr. Anaesth. 23(3), 242-9, (2013)

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Aprotinin reduces the procalcitonin rise associated with complex cardiac surgery and cardiopulmonary bypass. Maruna P, Klein AA, Kunstýř J, et al. Physiol. Res. 62(1), 27-33, (2013)

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Efficacy of aprotinin treatment on bilateral blunt chest trauma created in rabbits. Kaya H, Kafali ME, Aydin K, et al. J. Pak. Med. Assoc. 63(1), 32-7, (2013)

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Reduction in serine protease activity correlates with improved rosacea severity in a small, randomized pilot study of a topical serine protease inhibitor. Two AM, Hata TR, Nakatsuji T, et al. J. Invest. Dermatol. 134(4), 1143-5, (2014)

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Reply to the editor. Pagano D and Freemantle N J. Thorac. Cardiovasc. Surg. 146(3), 732, (2013)

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Clinical evidence from randomized trials, network meta-analyses, and conflicts of interests. Catalá-López F J. Thorac. Cardiovasc. Surg. 146(3), 731-2, (2013)

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EMA, transparency, and decision-making process. Rosén M Lancet 382(9886), 26-7, (2013)

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III. Aprotinin and cardiac surgery: a sorry tale of evidence misused. McMullan V and Alston RP Br. J. Anaesth. 110(5), 675-8, (2013)

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Safety of aprotinin in adult cardiac surgery: revisiting the validity of a mixed-treatment comparison meta-analysis. Catalá-López F J. Thorac. Cardiovasc. Surg. 145(2), 610, (2013)

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Placement of molecules in (not out of) the cell. Dauter Z Acta Crystallogr. D Biol. Crystallogr. 69(Pt 1), 2-4, (2013)

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Beynon, R.J. and Bond, J.S., ed. Proteolytic Enzymes: A Practical Approach, (1989), 247

Merck 14,757

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