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A4529

Sigma-Aldrich

Aprotinin

3-7 TIU/mg solid, lyophilized powder

Synonym(s):

BPTI, Bovine pancreatic trypsin inhibitor, Trasylol, Trypsin inhibitor (basic)

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About This Item

Empirical Formula (Hill Notation):
C284H432N84O79S7
CAS Number:
9087-70-1
Molecular Weight:
6511.44
EC Number:
232-994-9
MDL number:
MFCD00130541
UNSPSC Code:
12352202
NACRES:
NA.54

product name

Aprotinin from bovine lung, lyophilized powder, 3-7 TIU/mg solid

biological source

bovine lung

form

lyophilized powder

specific activity

3-7 TIU/mg solid

mol wt

~6,500

solubility

H2O: >10 mg/mL

UniProt accession no.

P00974

storage temp.

2-8°C

InChI key

ZPNFWUPYTFPOJU-UHFFFAOYSA-N

Gene Information

cow ... PTI(404172)

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Application

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A M Mahdy et al.
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)
D Baran et al.
Acta physiologica (Oxford, England), 186(3), 209-221 (2006-02-25)
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
Birte Treeck et al.
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
Ilaria Musante et al.
Experimental physiology, 104(6), 866-875 (2019-03-30)
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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Articles

Aprotinin

While aprotinin and bovine pancreatic trypsin inhibitor (BPTI) are the same protein sequence, the term aprotinin is typically used when describing the protein derived from bovine lung.

Protocols

Enzymatic Assay of Aprotinin

Objective: To standardize a procedure for the enzymatic assay of Aprotinin.

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