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9002-08-8

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9002-08-8 Structure

9002-08-8 Structure
IdentificationBack Directory
[Name]

TRYPSINOGEN
[CAS]

9002-08-8
[Synonyms]

TRYPSINOGEN
TRYPSINOGEN FROM BEEF PANCREAS
trypsinogen from bovine pancreas
Trypsinogen >2500 U/mg from bovine
Trypsinogen >2500U/mg from bovine pancreas
Trypsinogen, PMSF treated from bovine pancreas
[EINECS(EC#)]

232-651-3
[Molecular Formula]

C39H55N9O17
[MDL Number]

MFCD00466939
[MOL File]

9002-08-8.mol
[Molecular Weight]

921.9
Chemical PropertiesBack Directory
[storage temp. ]

2-8°C
[form ]

essentially salt-free, lyophilized powder
Safety DataBack Directory
[Symbol(GHS) ]


GHS08
[Signal word ]

Danger
[Hazard statements ]

H315-H319-H334
[Precautionary statements ]

P302+P352-P305+P351+P338
[Hazard Codes ]

Xn
[Risk Statements ]

36/37/38-42
[Safety Statements ]

22-24-26-36/37
[WGK Germany ]

3
[F ]

10-21
Hazard InformationBack Directory
[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.
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