Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the gastric mucosa, haemostasis is hampered by the acidity and peptic activity of the gastric juice and by the fibrinolytic activity of plasmin. The hostile intragastric environment may be responsible for the unsecure haemostasis, with episodes of rebleeds often seen in gastroduodenal haemorrhage. Secondly, the haemostatic mechanisms of the gastric mucosa are largely independent of platelet aggregation and thus rely mainly on the coagulation system, making the gastric mucosa a unique model to test haemorrhagic effects of anticoagulants. Using a rat gastric chamber technique, we studied bleeding times from induced gastric mucosal lesions after intravenous administration of unfractionated and low molecular weight heparins. The bleeding times were dose-dependently prolonged by all heparins. With unfractionated heparin, significant prolongation of the bleeding times was seen already at a dose of 75 anti-Factor Xa U/kg, proving that the present model is more sensitive than previous models. The bleeding time per unit dose of both Kabi 2165 (p less than 0.05) and enoxaparin (p less than 0.001) was significantly less than that of unfractionated heparin.
 ...
PMID:A new model to assess the haemorrhagic potential of various heparin preparations. 196 19

The activity of chymosin, plasmin, and Lactococcus lactis enzymes (cell envelope proteinase, intracellular peptidases, and glycolytic enzymes) were determined after 5-min exposures to pressures up to 800 MPa. Plasmin was unaffected by any pressure treatment. Chymosin activity was unaffected up to 400 MPa and decreased at 500 to 800 MPa. Fifty percent of control chymosin activity remained after the 800 MPa treatment. The lactococcal cell envelope proteinase (CEP) and intracellular peptidase activities were monitored in cell extracts of pressure-treated cells. A pressure of 100 MPa increased the CEP activity, whereas 200 MPa had no effect. At 300 MPa, CEP activity was reduced, and 400 to 800 MPa inactivated the enzyme. X-Prolyl-dipeptidyl aminopeptidase was insensitive to 5-min pressure treatments of 100 to 300 MPa, but was inactivated at 400 to 800 MPa. Aminopeptidase N was unaffected by 100 and 200 MPa. However, 300 MPa significantly reduced its activity, and 400 to 800 MPa inactivated it. Aminopeptidase C activity increased with increasing pressures up to 700 MPa. High pressure did not affect aminopeptidase A activity at any level. Hydrolysis of Lys-Ala-p-NA doubled after 300-MPa exposure, and was eliminated at 400 to 800 MPa. Glycolytic enzyme activities of pressure-treated cells were evaluated collectively by determining the titratable acidity as lactic acid produced by cell extracts in the presence of glucose. The titratable acidities produced by the 100 and 200 MPa samples were slightly increased compared to the control. At 300 to 800 MPa, no significant acid production was observed. These data demonstrate that high pressure causes no effect, activation, or inactivation of proteolytic and glycolytic enzymes depending on the pressure level and enzyme. Pressure treatment of cheese may alter enzymes involved in ripening, and pressure-treating L. lactis may provide a means to generate attenuated starters with altered enzyme profiles.
 ...
PMID:High pressure effects on proteolytic and glycolytic enzymes involved in cheese manufacturing. 1274 37