Trypsinogen

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1.What is the Trypsinogen ?

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 form 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.

2.What is the CAS number for Trypsinogen ?

The CAS number of Trypsinogen is 9002-08-8.

3.What are another words for Trypsinogen ?

Synonyms?for?Trypsinogen 9002-08-8:Anionictrypsinogen; Cationic trypsinogen; Prococoonase; Protrypsin; Streptogenosin;Trypsinogen 1; Trypsinogen 2

4.What is Trypsinogen (9002-08-8) used for?

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) microscopytuning and calibration of electrospray ionization quadrupole time-of-flight (ESI-Q-TOF) mass spectrometerthe secondary structure analysis of proteins by infrared (IR) spectroscopySDS-PAGE as a molecular weight standard (24kDa)

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