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.

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

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.

enterokinase

[en′tirōkī′nās]
Etymology: Gk, enteron + kinesis, movement, ase, enzyme
an intestinal juice enzyme that activates the proteolytic enzymes in pancreatic juice as they enter the duodenum.

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.

enterokinase

See ENTEROPEPTIDASE.

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.

enterokinase

the intestinal hormone that activates trypsinogen into becoming active trypsin.
References in periodicals archive ?
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.
Enterokinase or enteropeptidase is a heterodimeric serine protease produced by cells in the duodenal wall.
Preparation of recombinant thioredoxin fused N-terminal proCNP: analysis of enterokinase cleavage products reveals new enterokinase cleavage sites.
c) A recombinant proform of hK2 with a propeptide mutation in five of seven amino acids with increased stability and reduced activity that, because of the mutation, can be activated by enterokinase (ek-rhK2).
Trypsinogen and chymotrypsinogen in the homogenates were activated with enterokinase at a concentration of 4 mg/ml and incubated at 4[degrees]C for 24 h.