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Possible Interaction: Aprotinin and Chymotrypsin



Research Papers that Mention the Interaction

Third, the ability of aprotinin to neutralize, to varying degrees, the action of several serine proteases, such as trypsin, chymotrypsin , and particularly the urokinase-type plasminogen activator (uPA) and kallikreins is important, because these proteases have been implicated in tumor progression and development of metastasis.
Journal of the American College of Surgeons  •  2004  |  View Paper
The action of either chymotrypsin or trypsin was completely prevented by the serine protease inhibitor aprotinin , indicating that the proteolytic activity of the enzymes accounts for apoptosis induction.
Laboratory investigation; a journal of technical methods and pathology  •  1996  |  View Paper
Aprotinin is a potent antifibrinolytic that inhibits several serine proteases, specifically plasmin, trypsin, chymotrypsin , kallikrein, and thrombin.
Paediatric anaesthesia  •  2014  |  View Paper
Trasylol showed strong inhibitory effects on trypsin and chymotrypsin but also decreased thermolysin activity.
Islets  •  2010  |  View Paper
Aprotinin , a serine proteinase inhibitor, inhibits multiple proteases including plasmin, trypsin, kallikrein, chymotrypsin , activated protein C, and thrombin.
Journal of thrombosis and haemostasis : JTH  •  2006  |  View Paper
Fetal calf serum and aprotinin showed strong inhibitory actions toward trypsin and chymotrypsin.
Transplantation proceedings  •  2003  |  View Paper
When co-injected with chymotrypsin , the protease inhibitor aprotinin abolished the stimulatory effect of chymotrypsin on sodium reabsorption (31.7 ± 3.4% versus 32.1 ± 2.1%), while aprotinin alone had no effect.
Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association  •  2013  |  View Paper
Aditionally, the presence of a digestive chymotrypsin only partially inhibited by BSTI may provide an alternative path for proteolysis.
Journal of insect physiology  •  2008  |  View Paper
Camel chymotrypsin was more susceptible than its bovine equivalent to inhibition by soybean trypsin inhibitor and aprotinin.
Molecular and Cellular Biochemistry  •  2004  |  View Paper
Thus, the inhibitory properties of BPTI were improved by as much as 7 x 10(6)-fold towards elastase and 420-fold towards chymotrypsin.
Biochimica et biophysica acta  •  2001  |  View Paper
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