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A6012
Sigma-Aldrich
Aprotinin from bovine lung
saline solution, 5-10 TIU/mL
| Synonym: | Trypsin inhibitor (basic) |
| CAS Number: | 9087-70-1 |
| Linear Formula: | C284H432N84O79S7 |
| Molecular Weight: | 6511.44 |
| MDL number: | MFCD00130541 |
Description
| Analysis Note | Protein determined by biuret. |
| Another commonly used unit of activity is the KIU (Kallikrein Inhibitor Unit). 1 TIU ∼ 1,300 KIU. | |
| Unit Definition | 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- |
| Physical form | Solution in 0.9% NaCl and 0.9% benzyl alcohol. |
| Biochem/physiol Actions | Aprotinin is a competitive serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein and plasmin. Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin-protease complexes dissociating at pH >10 or <3. Effective concentration equimolar with protease. |
| General description | Aprotinin is a protein consisting of 58 amino acids, arranged in a single polypeptide chain that is crosslinked by three disulfide bridges. |
Properties
| sterility | aseptically filled |
| form | saline solution |
| mol wt | mol wt ~6,500 |
| concentration | 5-10 TIU/mL |
| storage temp. | 2-8°C |
Safety
| WGK Germany | NWG |
Related Products
| Replaced by | A6279, Aprotinin from bovine lung |
References
| reference | Deutscher, M.P., Maintaining protein stability. Meth. Enzymol. 182, 83-89, (1990) |
| Dignam, J.D., Preparation of extracts from higher eukaryotes. Meth. Enzymol. 182, 194-203, (1990) | |
| , Beynon, R.J. and Bond, J.S., ed. Proteolytic Enzymes: A Practical Approach, (1989), 247 | |
| Trautschold, I., et al. Biochem. Pharmacol. 16, 59, (1967) | |
| Gebhard, W., Review: Biochemistry of aprotinin and aprotinin-like inhibitors. Res. Monogr. Cell Tissue Physiol. 12, 375, (1986) | |
| Merck | Merck 13,761 |






