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Key Documents

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

Numero CAS:
Numero CE:
Codice UNSPSC:
12352202
NACRES:
NA.56

Origine biologica

bovine pancreas

Saggio

85-100% (UV)

Forma fisica

essentially salt-free, lyophilized powder

Attività specifica

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

PM

23,981 Da by calculation

tecniche

mass spectrometry (MS): suitable

Solubilità

H2O: soluble 10 mg/mL

N° accesso UniProt

Temperatura di conservazione

−20°C

Informazioni sul gene

bovine ... TRYP8(282603)

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Descrizione generale

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.

Applicazioni

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)

Azioni biochim/fisiol

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.

Definizione di unità

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).

Pittogrammi

Health hazard

Avvertenze

Danger

Indicazioni di pericolo

Classi di pericolo

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

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Faceshields, Gloves, type N95 (US)


Certificati d'analisi (COA)

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I clienti hanno visto anche

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Keil B, et al.
The Enzymes, 3, 250-275 null
Evidence for an active center histidine in trypsin through use of a specific reagent, 1-chloro-3-tosylamido-7-amino-2-heptanone, the chloromethyl ketone derived from Nα-tosyl-L-lysine.
Shae E, et al.
Biochemistry, 4, 2219-2224 (1965)
Trypsinogens and trypsins of various species.
Walsh K A, et al.
Methods in Enzymology, 19, 41-63 (1970)
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)
TRYPSINOGEN AND CHYMOTRYPSINOGEN AS HOMOLOGOUS PROTEINS.
K A WALSH et al.
Proceedings of the National Academy of Sciences of the United States of America, 52, 884-889 (1964-10-01)

Protocolli

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