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T1143 Sigma

Trypsinogen from bovine pancreas

essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein (E1%/280, after activation to trypsin)

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Properties

Related Categories Application Index, Biochemicals and Reagents, Enzymes, Inhibitors, and Substrates, Mass Spectrometry, Molecular Biology,
form   essentially salt-free, lyophilized powder
mol wt   mol wt 23,981 Da by calculation
solubility   H2O: soluble10 mg/mL
storage temp.   −20°C

Description

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.

Packaging

1 g in glass bottle

250 mg in glass bottle

Unit Definition

One BAEE unit is equal to a ΔA253 of 0.001 per min with BAEE as substrate at pH 7.6 at 25 °C and a reaction volume of 3.2 mL (1 cm light path).

Application

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)

Biochem/physiol Actions

Phytic acid complexed with calcium has been shown to increase the secretion of trypsinogen unable to be cleaved for activation. It also reduced the stabilization effect of calcium on activated trypsin. The active form of trypsinogen, referred to as trypsin, cleaves peptides on the C-terminal side of lysine and arginine amino acid residues. It also hydrolyzes ester and amide linkages of synthetic derivatives of amino acids such as, benzoyl L-arginine ethyl ester (BAEE), p-toluenesulfonyl-L-arginine methyl ester (TAME), etc.

Price and Availability

Safety & Documentation

Safety Information

Symbol 
GHS08  GHS08
Signal word 
Danger
Hazard statements 
Precautionary statements 
RIDADR 
NONH for all modes of transport
WGK Germany 
1

Documents

Certificate of Analysis

Certificate of Origin

Protocols & Articles

Protocols

Enzymatic Assay of Trypsinogen

This scope of this procedure applies to products that have a specification for the enzymatic activity of trypsinogen.
Keywords: Enzyme activity, Extinction coefficient

Enzymatic Assay of Urease from Jack Beans

The scope of this procedure is for all products that have a specification for the enzymatic determination of Urease, from Jack Beans. This assay is not to be used to determine the activity of Urease,...
Keywords: Indicators, Sonication, Titrations

Peer-Reviewed Papers
15

References

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