Trypsin inhibitor Chemical Properties

storage temp. 

-20°C

solubility 

H₂O: >10 mg/mL

form 

solution

color 

White to off-white

PH

<7.4

biological source

Phaseolus limensis (lima bean)

Water Solubility 

Soluble in water (10 mg/ml), phosphate buffers (10 mg/ml), and balanced salt solutions (1 mg/ml).

Specific Activity

≥7,000units/mg protein

Safety Information

Hazard Codes 

Xn

Risk Statements 

42/43

Safety Statements 

22-36/37-45-23

WGK Germany 

3

F 

10-21

HS Code 

35040090

Trypsin inhibitor Usage And Synthesis

Chemical Properties

It is a kinin release enzyme inhibitor extracted from bovine pancreas, lungs, gills and other tissues. It is not an enzyme itself, and is an alkaline polypeptide consisting of 58 amino acid residues, with the whole molecule in pear shape, and lysine as the active center. It can compete with the activity center of many proteases for a lysyl group and inhibit their activities. It is white or slightly yellow powder, odorless, soluble in water, dialyzable, with isoelectric point of 10-10.5. It is stable to high temperature, acid, alkali and enzyme. It is stable to high temperature, acid, alkali and enzyme. It can be heated to 100℃ in dilute acid, and it is still stable when placed at room temperature for 24h at pH12.6, but its vitality starts to decrease at pH12.8. In 60-80 ℃ can be thermophilic protease digestion, other enzymes can not inactivate it.

Uses

Trypsin Inhibitor, Corn is a specific reversible inhibitor of trypsin and potent inhibitor of human factor XIIa.

Uses

Trypsin inhibitor from chicken egg white has been used:

• to produce denatured, oxidized and deglycosylated ovomucoid and used to stimulate patient derived cell cultures for mapping T cell epitopes
• to treat nuclei for flow cytometric analysis
• in Holtfreter′s solution, used for the dissociation of planarians into cells

Uses

This product has been tested for cell culture applications. Trypsin has been used in a study to assess the potential application in animal cell culture of an alkaline protease from a ton-toxigenic mangrove isolate of Vibri sp. V26. Trypsin has also been used in a study to improve the detection of fungi in eosinophilic mucin.

General Description

Ovomucoid or trypsin inhibitor is an abundant protein in most avian egg whites. The hen′s egg protein is composed of about 186 amino acid residues, and is highly glycosylated. Three tandem domains are each homologous with pancreatic trypsin inhibitor. It is highly immunogenic, and probably accounts for most cases of egg allergy.

Biochem/physiol Actions

This inhibitor acts against trypsin, and chymotrypsin and plasmin to a lesser extent. It will also inhibit proteases with mechanisms similar to trypsin, plasma kallikrein and coagulation Factor X. The trypsin inhibitor will not act against metalloproteases, tissue-baseed kallikrein, acid proteases, or thio proteases. This inhibitor acts by forming a 1:1 stoichiometric complex with the protease active site, and then cleaving a single arginine-isoleucine bond on the inhibitor. The inhibition is both reversible and pH dependent.

Trypsin inhibitor(9035-81-8)Related Product Information

• Pepstatin
• CHYMOSTATIN
• Pancreatin
• TRYPSINOGEN
• Trypsin
• TRYPSIN FROM BOVINE PANCREAS
• RIBONUCLEASE INHIBITOR
• Ethyl isocyanoacetate
• Benzyl isocyanide
• Tosylmethyl isocyanide
• TERT-BUTYL ISOCYANIDE
• SALCOMINE
• N-BUTYLISOCYANIDE
• METHYL ISOCYANOACETATE
• Ferric acetylacetonate
• Tris(2,4-pentanedionato)chroMiuM(III)
• Aluminum acetylacetonate
• DICHLORO(ETHYLENEDIAMINE)PLATINUM(II)