Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.9 (enterokinase)
 675 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

It has been proposed that modulation of cholecystokinin (CCK) release by proteinases, proteinase inhibitors and protein is mediated by a pancreatic secretory trypsin inhibitor (PSTI), also called monitor peptide, in the rat. When human [125I]-PSTI was incubated with fasting small bowel juice or activated pancreatic juice greater than 88% of tracer eluted from gel chromatography in the characteristic position of hydrolysed PSTI. However, when the small bowel juice had been pre-incubated with soybean trypsin inhibitor 3 g/l, casein 5 g/l or lactalbumin 30 g/l, the hydrolysis of PSTI diminished so that 95%, 32%, and 33% respectively, now eluted in the characteristic position of free (i.e. intact and not bound to an enzyme) PSTI. When [125I]-PSTI was incubated with pure trypsin, chymotrypsin, elastase or enterokinase greater than 95% of tracer eluted in the position of PSTI-enzyme complex. Incubation of PSTI with trypsin plus one other enzyme was required to produce hydrolysis. The degree of protection of PSTI from hydrolysis in duodenal juice produced by these substances correlates with their affects on CCK release. Our findings support the hypothesis that PSTIs mediate the modulation of CCK release by intraluminal proteinases, proteinase inhibitors and proteins.
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PMID:Interactions of pancreatic secretory trypsin inhibitor in small intestinal juice: its hydrolysis and protection by intraluminal factors. 209 78

Forty-two samples were taken from the contents of the proximal small intestine of two lactating dairy cows fitted with re-entrant duodenal cannula. Most samples were free of detectable amylase activity. The (chymo)trypsinogen present was only partially activated to (chymo)trypsin. The activation was continued in vitro: slowly at the original pH of the samples (between pH 2.8 and 4.2), and faster after neutralization or a slight alkalinization. The effect of Ca, EDTA and soybean inhibitor on the activation of trypsinogen was also studied. The pancreatic enzymes were inactive in the acid pH range of the samples, but pepsin was markedly active. At pH 3.8 casein was digested rapidly by purified pepsin and slowly by the samples (agar-plate experiments). In model experiments performed with purified enzymes, pepsin digested (chymo)trypsin rapidly at pH 1-2 and slowly at pH 3.8. In the intestinal juice (chymo)trypsin and their zymogens seemed to be unaffected by pepsin under the conditions of the samples. It is concluded that the conditions prevailing in the duodenum/upper jejunum of the experimental cows account for a gastric-type digestion, despite the presence of pancreatic enzymes. In vivo the intestinal contents pass in distal direction. Meanwhile the pH of the chyme gradually increases and gives rise to first an increase of enterokinase activity accounting for a faster activation of the zymogens; second a start of function of activated pancreatic proteases and third a gradual decrease of pepsin activity and finally to its irreversible denaturation. Thus the development of intestinal type digestion is delayed in ruminants.
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PMID:Investigations about influence of the content of plant crude protein in the ration on the utilization of urea in dairy cattle. 6. Digestive enzymes and their interactions in contents of proximal small intestine. 643 91

A method is described for isolating a crystalline protein of high tryptic activity from beef pancreas. The protein has constant proteolytic activity and optical activity under various conditions and no indication of further fractionation could be obtained. The loss in activity corresponds to the decrease in native protein when the protein is denatured by heat, digested by pepsin, or hydrolyzed in dilute alkali. The enzyme digests casein, gelatin, edestin, and denatured hemoglobin, but not native hemoglobin. It accelerates the coagulation of blood but has little effect on the clotting of milk. It digests peptone prepared by the action of pepsin on casein, edestin or gelatin. The extent of the digestion of gelatin caused by this enzyme is the same as that caused by crystalline pepsin and is approximately equivalent to tripling the number of carboxyl groups present in the solution. The activity of the preparation is not increased by enterokinase. The molecular weight by osmotic pressure measure is about 34,000. The diffusion coefficient in (1/2) saturated magnesium sulfate at 6 degrees C. is 0.020 +/-0.001 cm.(2) per day, corresponding to a molecular radius of 2.6 x 10(-7) cm. The isoelectric point is probably between pH 7.0 and pH 8.0. The optimum pH for the digestion of casein is from 8.0-9.0. The optimum stability is at pH 1.8.
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PMID:CRYSTALLINE TRYPSIN : II. GENERAL PROPERTIES. 1987 6

A new crystalline protein, chymo-trypsinogen, has been isolated from acid extracts of fresh cattle pancreas. This protein is not an enzyme but is transformed by minute amounts of trypsin into an active proteolytic enzyme called chymo-trypsin. The chymo-trypsin has also been obtained in crystalline form. The chymo-trypsinogen cannot be activated by enterokinase, pepsin, inactive trypsin, or calcium chloride. There is an extremely slow spontaneous activation upon standing in solution. The activation of chymo-trypsinogen by trypsin follows the course of a monomolecular reaction the velocity constant of which is proportional to the trypsin concentration and independent of the chymotrypsinogen concentration. The rate of activation is a maximum at pH 7.0-8.0. Activation is accompanied by an increase of six primary amino groups per mole but no split products could be found, indicating that the activation consists in an intramolecular rearrangement. There is a slight change in optical activity but no change in molecular weight. The physical and chemical properties of both proteins are constant through a series of fractional crystallizations. The activity of chymo-trypsin decreases in proportion to the destruction of the native protein by pepsin digestion or denaturation by heat or acid. Chymo-trypsin has powerful milk-clotting power but does not clot blood plasma and differs qualitatively in this respect from the crystalline trypsin previously reported. It hydrolyzes sturin, casein, gelatin, and hemoglobin more slowly than does crystalline trypsin but the hydrolysis of casein is carried much further. The hydrolysis takes place at different linkages from those attacked by trypsin. The optimum pH for the digestion of casein is about 8.0-9.0. It does not hydrolyze any of a series of dipeptides or polypeptides tested. Several chemical and physical properties of both proteins have been determined.
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PMID:CRYSTALLINE CHYMO-TRYPSIN AND CHYMO-TRYPSINOGEN : I. ISOLATION, CRYSTALLIZATION, AND GENERAL PROPERTIES OF A NEW PROTEOLYTIC ENZYME AND ITS PRECURSOR. 1987 56

1. Methods for the preparation and partial purification of streptococcal fibrinolysin are described. 2. The lysis of fibrin clots in the presence of streptococcal fibrinolysin is associated with proteolysis of the fibrin. Digestion is due to an enzyme normally present in serum or plasma in an inactive state, which is activated by fibrinolysin. Fibrinolysin alone has no demonstrable proteolytic activity. 3. The lysin factor-fibrinolysin system brings about proteolysis of other proteins such as gelatin or casein, in addition to fibrin and fibrinogen. 4. It is suggested that lysin factor exists in serum or plasma as a zymogen, and that it is activated by fibrinolysin, a kinase, in a manner similar to the activation of trypsinogen by enterokinase or the mold kinase of Kunitz (1938).
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PMID:STREPTOCOCCAL FIBRINOLYSIS: A PROTEOLYTIC REACTION DUE TO A SERUM ENZYME ACTIVATED BY STREPTOCOCCAL FIBRINOLYSIN. 1987 27

1. Fibrinolysin-activated lysin factor and chloroform-activated serum protease of serum and plasma are one and the same enzyme, differing only in their mode of activation. 2. The enzyme as it normally occurs in serum or plasma is not inactive because of combination with serum inhibitor. It is present as an inactive precursor or zymogen and may be activated from this state by streptococcal fibrinolysin. 3. The activation of serum protease by streptococcal fibrinolysin is a catalytic reaction, analogous to the kinase activation of trypsinogen by enterokinase. Treatment of serum or plasma with chloroform apparently results in removal of serum inhibitor which may allow autocatalytic activation of the serum protease. 4. The serum enzyme differs from trypsin in its pH of optimum activity, in its reactions with specific protease inhibitors, and in its action on casein. 5. A revised nomenclature for the serum enzyme system is suggested which more accurately describes its properties than the terms in current use.
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PMID:A PROTEOLYTIC ENZYME OF SERUM: CHARACTERIZATION, ACTIVATION, AND REACTION WITH INHIBITORS. 1987 36