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Merck

T1143

Sigma-Aldrich

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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About This Item

Número de CAS:
Número CE:
Código UNSPSC:
12352202
NACRES:
NA.56

origen biológico

bovine pancreas

Nivel de calidad

Ensayo

85-100% (UV)

Formulario

essentially salt-free, lyophilized powder

actividad específica

≥10,000 BAEE units/mg protein (E1%/280, after activation to trypsin)

mol peso

23,981 Da by calculation

técnicas

mass spectrometry (MS): suitable

solubilidad

H2O: soluble 10 mg/mL

Nº de acceso UniProt

temp. de almacenamiento

−20°C

Información sobre el gen

bovine ... TRYP8(282603)

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Descripción general

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.

Aplicación

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)

Acciones bioquímicas o fisiológicas

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.

Definición de unidad

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).

Pictogramas

Health hazard

Palabra de señalización

Danger

Frases de peligro

Clasificaciones de peligro

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Faceshields, Gloves, type N95 (US)


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Visite la Librería de documentos

An effect of calcium ions on the activity, heat stability, and structure of trypsin.
T Sipos et al.
Biochemistry, 9(14), 2766-2775 (1970-07-07)
The effect of calcium and phytic acid on the activation of trypsinogen and stability of trypsin.
Caldwell, R.
Journal of Agricultural and Food Chemistry, 40, 43-46 (1992)
Thomas M Dillon et al.
Journal of chromatography. A, 1053(1-2), 299-305 (2004-11-17)
Analytical characterization of monoclonal antibodies has been hindered by the lack of appropriate chromatographic methods to be used in conjunction with high-resolution MS. Current methodologies for standard RP-HPLC are incompatible with antibodies due to irreproducibility, low recovery, short column lifetimes
Rapid analysis of single-cysteine variants of recombinant proteins.
T W Keough et al.
Methods in molecular biology (Clifton, N.J.), 61, 171-183 (1996-01-01)
Keil B, et al.
The Enzymes, 3, 250-275 null

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