9002-08-8

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)

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.

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