Enteropeptidase (also alleged
enterokinase) is an agitator produced by beef of the duodenum and complex in
beastly and beastly digestion. It is buried from abdominal glands (the crypts
of Lieberkühn) afterward the access of ingested aliment casual from the
stomach. Enteropeptidase converts trypsinogen (a zymogen) into its alive
anatomy trypsin, consistent in the consecutive activation of pancreatic
digestive enzymes.Absence of enteropeptidase after-effects in abdominal
assimilation impairment.
Enteropeptidase is a serine
protease (EC 3.4.21.9) consisting of a disulfide-linked heavy-chain of 82-140
kDa that anchors enterokinase in the abdominal besom bound film and a
light-chain of 35–62 kDa that contains the catalytic subunit. Enteropeptidase
is a allotment of the chymotrypsin-clan of serine proteases, and is
structurally agnate to these proteins.
Enteropeptidase's specificity
makes it an ideal apparatus in biochemical applications; a admixture protein
absolute a C-terminal affection tag (such as poly-His) affiliated by this
arrangement can be broken by enteropeptidase to access the ambition protein
afterward protein purification. On the converse, the N-terminal pro-sequence of
proteases that have to be broken above-mentioned to activation can be mutated
to accredit activation with enteropeptidase.
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