Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.21.9 (
enterokinase
)
675
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Chymotrypsin
, trypsin, carboxypeptidase A and B, elastase and
enterokinase
activities were measured in buffer solutions and in human duodenal juice after incubation with wheat bran, cellulose, guar gum, pectin, psyllium and lignin. The different types of dietary fiber led to inhibition of enzymatic activity in most experiments, e.g., lignin could totally ablish the activity of isolated trypsin and chymotrypsin. Only in
enterokinase
was there no influence. Inhibition depended on incubation time; the effect was proportional to fiber concentration and inversely related to enzyme level. Treatment of fiber with hydrochloric acid (pH 1.5) and heat (95 degrees C) destroyed inhibitory activity in some experiments. The effect of lignin on one enzyme (trypsin) was reduced by the addition of another enzyme (chymotrypsin). It is concluded that dietary fiber could affect digestion by inhibiting proteolytic pancreatic enzymes.
...
PMID:Effect of dietary fiber on proteolytic pancreatic enzymes in vitro. 282 29
The quantitative release of
enterokinase
from isolated rat enterocytes following treatment with taurocholate-taurodeoxycholate, papain, chymotrypsin, elastase, carbamylcholine, and cholecystokinin-octapeptide was examined. Alkaline phosphatase and lactate dehydrogenase activities were evaluated simultaneously to check for specificity. Bile salts promoted a concentration-dependent release of all enzymes. Concomitantly, bile salts also led to cell destruction in proportion to the amount of enzymes released. Proteases caused the release of
enterokinase
and alkaline phosphatase with no concomitant increase of lactate dehydrogenase or cell lysis. At equal concentrations, papain released more enzymes than chymotrypsin and elastase.
Chymotrypsin
and elastase, however, led to higher ratios of
enterokinase
to alkaline phosphatase found in the media and suggested a selective release of
enterokinase
(EK) over that of alkaline phosphatase. Bile salts and pancreatic proteases together seem to have an additive effect of the release of EK. Carbamylcholine and cholecystokinin-octapeptide had no effect on enzyme release. These results suggested that pancreatic proteases are involved in the release of
enterokinase
by a selective action. Bile salts may also play a role through a nonselective detergent effect.
...
PMID:Physiological factors controlling release of enterokinase from rat enterocytes. 390 6
