enterokinase


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Related to enterokinase: secretin, enterokinase deficiency

enteropeptidase

 [en″ter-o-pep´tĭ-dās]
an enzyme of the intestinal juice secreted by the duodenal mucosa; it activates the proteolytic enzyme of the pancreatic juice by converting trypsinogen into trypsin.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

en·ter·o·pep·ti·dase

(en'tĕr-ō-pep'ti-dās),
An intestinal proteolytic glycoenzyme from the duodenal mucosa that converts trypsinogen into trypsin (removes a hexapeptide from trypsinogen).
Synonym(s): enterokinase
Farlex Partner Medical Dictionary © Farlex 2012

enterokinase

(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.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.

TMPRSS15

A gene on chromosome 21q21 that encodes a serine protease responsible for activating pancreatic proteolytic proenzymes by catalysing the conversion of trypsinogen to trypsin, which in turn activates other proenzymes, including chymotrypsinogen, procarboxypeptidases and proelastases. It is localised at the intestinal brush border.

Molecular pathology
Defects in TMPRSS15 are a cause of enterokinase deficiency.
Segen's Medical Dictionary. © 2012 Farlex, Inc. All rights reserved.

enterokinase

See ENTEROPEPTIDASE.
Collins Dictionary of Medicine © Robert M. Youngson 2004, 2005

enterokinase

see ENTEROPEPTIDASE.

enterokinase

) an ENZYME secreted by cells of the DUODENUM, which catalyses the conversion of inactive TRYPSINOGEN in the PANCREATIC JUICE to active TRYPSIN.
Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005
References in periodicals archive ?
(D) The fusion peptide and its cleaved forms by enterokinase. M, protein markers; Lane 1, pBD-2/cecropin P1 fusion peptide; Lane 2, pBD-2 (6 kDa) and cecropin P1 (8 kDa) peptides generated from the fusion peptide by enterokinase digestion.
By performing the previously described pilot digestion experiments, optimal cleavage was observed by using native enterokinase at protein: protease mass ratio of 1:20 after overnight incubation at room temperature.
Surprisingly, we found that the fusion proteins obtained from insect cells were resistant to enterokinase independently of the enzyme source and experimental conditions, whereas the proteins isolated from E.
However, we are more inclined to explain the enterokinase resistance of the fusion protein from insect cells with the specific posttranslational glycosylation of hIFN[gamma] proteins.
In this paper we describe the negative effect of the N-terminal [His.sub.6]-FLAG tag on the biological activity of two proteins with therapeutic application (hIFN[gamma] and its mutant K88Q) and its resistance to enterokinase digestion when the proteins are glycosylated.
Seong, "Recombinant enterokinase light chain with affinity tag: expression from Saccharomyces cerevisiae and its utilities in fusion protein technology," Biotechnology and Bioengineering, vol.
Janska, "Enterokinase (enteropeptidase): comparative aspects," Trends in Biochemical Sciences, vol.
Lim et al., "An SRLLR motif downstream ofthe scissile bond enhances enterokinase cleavage efficiency," Biochimie, vol.
Shin, "Enhancing the specificity of the enterokinase cleavage reaction to promote efficient cleavage of a fusion tag," Protein Expression and Purification, vol.
Then, the fusion partner with 18 kDa, was separated from rhPTH through digestion with enterokinase (Figure 3).