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.
American Heritage® Dictionary of the English Language, Fifth Edition. Copyright © 2016 by Houghton Mifflin Harcourt Publishing Company. Published by Houghton Mifflin Harcourt Publishing Company. All rights reserved.

enterokinase

(ˌɛntərəʊˈkaɪneɪz)
n
(Biochemistry) an enzyme in intestinal juice that converts trypsinogen to trypsin
Collins English Dictionary – Complete and Unabridged, 12th Edition 2014 © HarperCollins Publishers 1991, 1994, 1998, 2000, 2003, 2006, 2007, 2009, 2011, 2014

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]
Random House Kernerman Webster's College Dictionary, © 2010 K Dictionaries Ltd. Copyright 2005, 1997, 1991 by Random House, Inc. All rights reserved.
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
Based on WordNet 3.0, Farlex clipart collection. © 2003-2012 Princeton University, Farlex Inc.
Translations
entérokinase
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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.
Construction of Bacillus subtilis strain engineered for expression of porcine [beta]-defensin-2/cecropin P1 fusion antimicrobial peptides and its growth-promoting effect and antimicrobial activity
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.
Gene Expression and Molecular Characterization of a Xylanase from Chicken Cecum Metagenome
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.
His-FLAG Tag as a Fusion Partner of Glycosylated Human Interferon-Gamma and Its Mutant: Gain or Loss?
Enterokinase possesses trypsin-like activity and specifically cleaves after lysine residue at a canonical recognition sequence (DDDDKX) [55].
Several affinity tags commonly used in chromatographic purification
Furthermore, with PG, the pancreatic exocrine secretions enter the acidic gastric environment, where the low pH and lack of enterokinase prevent their activation.
Evaluation of a new modification of pancreaticogastrostomy after pancreaticoduodenectomy: anastomosis of the pancreatic duct to the gastric mucosa with invagination of the pancreatic remnant end into the posterior gastric wall for patients with cancer head of pancreas and periampullary carcinoma in terms of postoperative pancreatic fistula formation
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).
The discovery of insulin: a case study of scientific methodology
After secretion into the gastrointestinal tract, they are activated to trypsins (EC 3.4.21.4) by enterokinase (3).
Specific immunoassay reveals increased serum trypsinogen 3 in acute pancreatitis
[25] Jacob, R, T., "et al" 1983, "Isolation and Characterization of a specific enterokinase inhibitor from kidney bean (Phaseolus vulgaris) "Biochem.
Evidence of fibrinolytic protease in the latex of Synadenium grantii Hook 'f'
The N-terminal thioredoxin/6xhis-tag was removed by cleavage with recombinant enterokinase (Novagen, Madison, WI, USA) according to the manufacturer's recommendations.
Increase in pilus islet 2-encoded pili among Streptococcus pneumoniae isolates, Atlanta, Georgia, USA
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.
The evolution of enzyme treatment adopted from The Trophoblast and the Origins of Cancer

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