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At least 703 records · Page 39Linked to original sources
PubMed1981

The interaction between rat plasma alpha 1 inhibitor 3 and chymotrypsin. A protease-protease inhibitor system which gives partially active complexes.

Complexation of chymotrypsin with rat alpha 1 inhibitor 3 (alpha 1I3) leads to a significant modification of circular dichroism (CD) spectra in the near ultraviolet. These spectra variations are due to structural changes of the inhibitor resulting from partial proteolysis. Taking advantage of this change in CD spectral properties a 1:1 stoichiometric ratio was determined for the interaction. However, when an excess of inhibitor was present in the mixture, a slow change of the CD spectrum was observed. This was shown to result from a partial proteolysis of native inhibitor identical to that occurring during complex formation. This hydrolysis was due to the remaining activity of the bound enzyme since no significant release of free enzyme from the complex was demonstrated. Addition of human alpha 1 proteinase inhibitor (alpha 1 Pi) to dissociate the complex resulted in the formation of an enzymatically inactive ternary complex which gave evidence for the stability of the alpha 1I3 chymotrypsin binding.

Acute-Phase Proteins↗
PubMed1988

[Effects of E-3123, a new protease inhibitor, on several protease activities and on experimental acute pancreatitis].

4-(2-Succinimidoethylthio) phenyl 4-guanidinobenzoate (E-3123) potently inhibited trypsin, plasmin and thrombin with IC50 values of 3.9 x 10(-8) M, 9.5 x 10(-7) M and 1.9 x 10(-6) M, respectively. Experimental acute pancreatitis was induced by injection of a mixture of trypsin and taurocholate into the pancreas in rats and rabbits or by an application of a closed duodenal loop in dogs. Intravenous infusion of E-3123 at 0.03-0.3 mg/kg in rats or at 0.3-3.0 mg/kg in rabbits reduced mortality after the induction of pancreatitis in a dose-dependent manner. Light microscopy of the pancreas in the E-3123-treated rabbits revealed marked decrease in cell necrosis and acinar cell vacuolation. Increase in plasma lipase activities associated with the progression of pancreatitis in rabbits was also reduced by the infusion of E-3123. In dogs with pancreatitis, increases in serum trypsin and lipase activities were significantly reduced by infusion of E-3123 at 1.0 and 3.0 mg/kg. The efficacies of E-3123 in the in vivo experiments were higher than those of nafamostat mesilate. These results show that E-3123 may possess suppressing effects on pathogenesis and development of acute pancreatitis.

Acute Disease↗