Synonym: Trasylol, Trypsin inhibitor (basic)
|Related Categories||Biochemicals and Reagents, Enzyme Inhibitors, Enzyme Inhibitors by Type, Enzymes, Inhibitors, and Substrates, Proteins More...|
|mol wt||mol wt ~6,500|
Another commonly used unit of activity is the KIU (Kallikrein Inhibitor Unit).
1 TIU ∼ 1,300 KIU.
A further purification of A1153 to yield a product with slightly higher activity and purity
One trypsin inhibitor unit (TIU) will decrease the activity of 2 trypsin units by 50% where one trypsin unit will hydrolyze 1.0 μmole of N-α-benzoyl-
Aprotinin is a protein consisting of 58 amino acids, arranged in a single polypeptide chain that is crosslinked by three disulfide bridges.
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recombinant, expressed in Nicotiana, ≥5 TIU/mg protein, ≥98% (SDS-PAGE)
lyophilized, ~80% (HPCE), crystalline (fine), white, ≥3500 U/mg
saline solution, 3-7 TIU/mg protein
lyophilized powder, 3-8 TIU/mg solid
lyophilized powder, 3-7 TIU/mg solid
2. SCOPE The scope of this procedure is all products that have a specification for Aprotinin activity.
Keywords: Enzymology, Extinction coefficient
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)
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)
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)
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)
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)
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)
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)
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)
Beynon, R.J. and Bond, J.S., ed. Proteolytic Enzymes: A Practical Approach, (1989), 247
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