Cat No.
NATE-0225
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)
Source
Porcine intestine
Species
Porcine
Form
salt-free, lyophilized powder
Enzyme Commission Number
EC 3.4.21.9
Bio-activity
Type I, > 20 units/mg protein
CAS No.
9014-74-8
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.
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.
Gene Name
TMPRSS15 transmembrane protease, serine 15 [Sus scrofa]
Synonyms
enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8
GeneID
397152
mRNA Refseq
NM_001001259
Protein Refseq
NP_001001259
UniProt ID
P98074
Chromosome Location
chromosome: 13
Function
scavenger receptor activity; serine-type endopeptidase activity
