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A1153

Aprotinin

3-8 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
UNSPSC Code:
12352202
NACRES:
NA.77
EC Number:
232-994-9
MDL number:
MFCD00130541
eCl@ss:
32190102
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Product Name

Aprotinin from bovine lung, lyophilized powder, 3-8 TIU/mg solid

biological source

bovine lung

Quality Level

300

form

lyophilized powder

specific activity

3-8 TIU/mg solid

mol wt

~6,500

solubility

H2O: ≥5 mg/mL

UniProt accession no.

P00974

storage temp.

2-8°C

SMILES string

S1SCC2NC(=O)CNC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C5NC(=O)C(NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C(NC(=O)C9N(CCC9)C(=O)CNC(=O)C(NC(=O)C(NC(=O)C%11N(CCC%11)C(=O

InChI

1S/C284H432N84O79S7/c1-21-144(9)222-271(439)337-174(68-46-105-309-282(300)301)239(407)340-187(120-160-77-85-164(374)86-78-160)251(419)341-185(116-156-55-29-24-30-56-156)250(418)342-188(121-161-79-87-165(375)88-80-161)252(420)346-191(123-208(291)378)246(41

InChI key

ZPNFWUPYTFPOJU-UHFFFAOYSA-N

Gene Information

cow ... PTI(404172)

General description

Aprotinin from bovine lung is a globular polypeptide monomer with a molecular weight of 6.5 kDa. Commonly used as a non-specific serine protease inhibitor, aprotinin contains an antiparallel β sheet, N-terminal 310 helix and C-terminal and α helix. Aprotinin residues from amino acids 13 - 18 are essential for binding to serine proteases.

Application

Aprotinin from bovine lung has been used:
  • as a protease inhibitor in radioimmunoprecipitation assay buffer (RIPA) for the homogenization of cardiac microvascular endothelial cells (CMECs)(4) and mammary epithelial cells
  • in angiogenesis assay for fibroblast
  • in the proteomic stabilization of saliva supernatant

Aprotinin is largely used as an inhibitor of trypsin.

Biochem/physiol Actions

Aprotinin inhibits proteases like trypsin, plasmin, chymotrypsin and thrombin. It blocks the bradykinin synthesis from kininogen. It is useful for treating blood loss during surgery.
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.

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.

Other Notes

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.

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Storage Class

11 - Combustible Solids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Protocols

Enzymatic Assay of Aprotinin

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

Articles

Elastase Function and Importance

Elastase application index for understanding leukocyte elastase, a 29KDa serine endoprotease.

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.

Chymotrypsin

Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.

View All Articles
Engineering of a biomimetic pericyte-covered 3D microvascular network
Kim J,
PLoS ONE, 10(7), e0133880-e0133880 (2015)
The effects of cell death-inducing DNA fragmentation factor-alpha-like effector C (CIDEC) on milk lipid synthesis in mammary glands of dairy cows
Yang Y, et al.
Journal of Dairy Science, 100(5), 4014-4024 (2017)
Perioperative systemic haemostatic agents
Mahdy AM and Webster NR
British journal of anaesthesia, 93(6), 842-858 (2004)
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Global Trade Item Number

SKUGTIN
A1153-100MG04061835551071
A1153-250MG04061835511273
A1153-10MG04061835511266
A1153-1MG04061835551088
A1153-25MG04061835511280
A1153-5MG04061835540501