Aprotinin is largely used as an inhibitor of trypsin.
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.
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 N-alpha-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.
Preparation Note
This product is an affinity purified lyophilized powder purified to remove trace impurities. It has an activity of 3-7 TIU/mg.
British journal of anaesthesia, 93(6), 842-858 (2004-07-28)
Skilful surgery combined with blood-saving methods and careful management of blood coagulation will all help reduce unnecessary blood loss and transfusion requirements. Excessive surgical bleeding causes hypovolaemia, haemodynamic instability, anaemia and reduced oxygen delivery to tissues, with a subsequent increase
Hemostatic drugs.
P M Mannucci
The New England journal of medicine, 339(4), 245-253 (1998-07-23)
The Journal of physiology, 541(Pt 3), 1049-1057 (2002-06-18)
Different changes in glomerular filtration rates (GFR) in deep and superficial glomeruli have been suggested to influence renal NaCl excretion and concentrating ability. Angiotensin II (AngII) has been implicated in such changes, but the experimental evidence has been conflicting, probably
The renal tubular uptake of 125I-Aprotinin (*Ap) is on average located more superficially than its filtration site, causing transfer of some of *Ap filtered in deep to more superficial cortical zones. 125I-Cystatin C (*Cy) showed less uptake in deep cortical
What is the central question of this study? What is the precise subcellular localization of the epithelial sodium channel (ENaC) in human airway epithelium? What is the main finding and its importance? ENaC protein has an unexpected localization in the
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