enterokinase


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Related to enterokinase: secretin, enterokinase deficiency

en·ter·o·ki·nase

 (ĕn′tə-rō-kī′nās′, -nāz′, -kĭn′ās′, -āz′)
n.
An enzyme secreted by the upper intestinal mucosa that catalyzes the conversion of trypsinogen to trypsin. Also called enteropeptidase.

enterokinase

(ˌɛntərəʊˈkaɪneɪz)
n
(Biochemistry) an enzyme in intestinal juice that converts trypsinogen to trypsin

en•ter•o•ki•nase

(ˌɛn tə roʊˈkaɪ neɪs, -neɪz, -ˈkɪn eɪs, -eɪz)
n.
an enzyme of the intestinal mucosa that promotes the conversion of trypsinogen into trypsin.
[1900–05]
ThesaurusAntonymsRelated WordsSynonymsLegend:
Noun1.enterokinase - enzyme in the intestinal juice that converts inactive trypsinogen into active trypsin
enzyme - any of several complex proteins that are produced by cells and act as catalysts in specific biochemical reactions
Translations
entérokinase
References in periodicals archive ?
For pBD-2 and cecropin P1 recovery, the purified pBD-2/cecropin P1 fusion peptides were digested with enterokinase (5 units/[micro]g of fusion peptide) to cleave the fusion protein to release the pBD-2 and cecropin P1.
The purified fusion protein was digested with enterokinase to remove the peptide tags and subjected to second round of purification to yield the purified mature [XynA.sub.MG1] enzyme for characterization experiments.
In the present paper we report and discuss our findings on the negative effect of [His.sub.6]-FLAG tag on the biological activity of the purified hIFN[gamma] and K88Q and its resistance to enterokinase digestion when the proteins were expressed as glycoproteins in insect cell line.
Enterokinase possesses trypsin-like activity and specifically cleaves after lysine residue at a canonical recognition sequence (DDDDKX) [55].
Trypsin is secreted as the zymogen trypsinogen; it is converted in the intestine into the active enzyme trypsin by an enzyme called enterokinase. The endocrine cells of the pancreas form small clusters throughout the organ called islets or islands of Langerhans (named for Paul Langerhans, who discovered them in 1869).
After secretion into the gastrointestinal tract, they are activated to trypsins (EC 3.4.21.4) by enterokinase (3).
[25] Jacob, R, T., "et al" 1983, "Isolation and Characterization of a specific enterokinase inhibitor from kidney bean (Phaseolus vulgaris) "Biochem.
The N-terminal thioredoxin/6xhis-tag was removed by cleavage with recombinant enterokinase (Novagen, Madison, WI, USA) according to the manufacturer's recommendations.
In the duodenum the intestinal enzyme enterokinase secreted by the mucosal cells cleaves off a small six amino acid terminal from trypsinogen, converting the precursor into the active enzyme.