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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-761-1
NACRES:
NA.54
MDL number:
Numéro CE :
Specific activity:
≥0.5 units/mg solid
Service technique
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salt-free, lyophilized powder
Quality Segment
specific activity
≥0.5 units/mg solid
mol wt
150 kDa
storage temp.
−20°C
Application
The enzyme from Sigma has been used for the activation of trypsinogen in order to measure the activity of trypsin in hog pancreas. The study showed that antimicrobial treatment reduces intestinal microflora and improves protein digestive capacity without changes in villous structure of weanling pigs.
Enterokinase from porcine intestine has been used in a study to report a new experimental model of the anomalous pancreatico-biliary junction. Enterokinase from porcine intestine has also been used in a study to investigate the insulinotropic region of the gastric inhibitory polypeptide.
Biochem/physiol Actions
Enterokinase is a membrane bound serine protease that specifically and rapidly converts trypsinogen to trypsin, thereby, triggering the conversion of other zymogens to active enzymes. It has a molecular mass of approximately 150 kDa. The enzyme is a heterodimer consisting of 35-47 kDa subunits. The light and the heavy chains are linked by two disulfide bridges. It is a glycoprotein containing 35% carbohydrate. The polypeptide chain of trypsinogen is hydrolyzed only after an -(Asp)4-Lys- sequence. The enzyme is inhibited by soybean trypsin inhibitor. Enterokinase is typically used in protein modification and amino acid sequence determination.
Other Notes
One unit will produce 1.0 nanomole of trypsin from trypsinogen per min at pH 5.6 at 25 °C.
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Classe de stockage
11 - Combustible Solids
Que se passe-t-il ?
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
EPI (équipement de protection individuelle)
Eyeshields, Gloves, type N95 (US)
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