TRYPSINOGEN Property

storage temp. 

2-8°C

form 

essentially salt-free, lyophilized powder

Safety

Hazard Codes 

Xn

Risk Statements 

36/37/38-42

Safety Statements 

22-24-26-36/37

WGK Germany 

3

F 

10-21

Hazard and Precautionary Statements (GHS)

Symbol(GHS)

Signal word

Danger

Hazard statements

H315Causes skin irritation

H319Causes serious eye irritation

H334May cause allergy or asthma symptoms or breathing difficulties if inhaled

Precautionary statements

P302+P352IF ON SKIN: wash with plenty of soap and water.

P305+P351+P338IF IN EYES: Rinse cautiously with water for several minutes. Remove contact lenses, if present and easy to do. Continuerinsing.

TRYPSINOGEN Chemical Properties,Usage,Production

Uses

Trypsinogen from bovine pancreas is suitable for use in:

• the secondary structure analysis of proteins in H2O solution using single-pass attenuated total reflection Fourier transform infrared (ATR-FT-IR) microscopy
• tuning and calibration of electrospray ionization quadrupole time-of-flight (ESI-Q-TOF) mass spectrometer
• the secondary structure analysis of proteins by infrared (IR) spectroscopy
• SDS-PAGE as a molecular weight standard (24kDa)

General Description

Trypsinogen is a proenzyme (zymogen) that is activated to form trypsin. It is synthesized in the pancreas and activated by enterokinase once it reaches the lumen of the small intestine. Bovine trypsinogen is a single polypeptide chain of 229 amino acids that is cross linked by six disulfide bridges. Enterokinase cleaves a hexapeptide to from the NH₂ terminus of trypsinogen at the Lys6 - Ile7 peptide bond and activates it. Trypsin, thus formed, autocatalytically activates more trypsinogen to trypsin. This native form of trypsin is called β-trypsin, which undergoes autolysis at Lys₁₃₁ - Ser₁₃₂ resulting in α-trypsin that is held together by disulfide bridges. Trypsin is a serine protease with His₄₆ and Ser₁₈₃ at the active site. The pH optimum of trypsin is 7 - 9.

Biochem/physiol Actions

Hereditary pancreatitis was shown to be caused by a Arg-His substitution at residue 117 of trypsinogen causing auto-activation of trypsinogen to trypsin.