Enterokinase


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Related to Enterokinase: secretin, enterokinase deficiency

enterokinase

[‚ent·ə·rō′kī‚nās]
(biochemistry)
An enzyme which catalyzes the conversion of trypsinogen to trypsin.

Enterokinase

 

a proteolytic enzyme of the class of endopeptidases. Enterokinase is a complex protein containing carbohydrates (glycoprotein). It has been discovered in man and some other mammals. The enzyme is secreted by cells of the mucosa of the duodenum into the lumen of the intestine, where it activates trypsinogen, which enters through the pancreatic duct. The enzyme trypsin thus formed activates trypsinogen and all the other proteolytic enzymes of pancreatic secretion. The direct participation of enterokinase in the digestion of food is insignificant, since only an extremely small quantity is present.

References in periodicals archive ?
However, the enterokinase cleavage site is only partially a ccessible to the enzyme.
Recombinant Bovine enterokinase, also known as enteropeptidase, is a specific protease used for tag removal, while V8 Protease (Endoproteinase GluC) is highly important for protein structure and sequence analysis.
64 ng/L, and we observed no cross-reactivity or interference with atrial natriuretic peptide (ANP), enterokinase, human airway trypsinlike protease, hepsin, LDL receptor, matriptase, spinesin, or seipins.