Description
Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment.
Abbr
Enterokinase, Native (Porcine)
Applications
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. The enzyme from Creative Enzymes 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.
Form
salt-free, lyophilized powder
Enzyme Commission Number
EC 3.4.21.9
Activity
Type I, > 20 units/mg protein
Composition
Protein, > 20% Lowry
Unit Definition
One unit will produce 1.0 nanomole of trypsin from trypsinogen per min at pH 5.6 at 25°C.
Function
scavenger receptor activity; serine-type endopeptidase activity
Synonyms
enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8
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