Abstract:
The association of porcine trypsin with soybean trypsin inhibitor (Kunitz) resulted in characteristic changes in absorption spectrum, indicating an alteration of the micro environments of the enzyme chromophores as a consequence of the _interaction. The rates of formation of the stable trypsin - inhibitor complexes from porcine -a- trypsin and soybean trypsin inhibitor and from porcine p- trypsin and either intact or modified soybean trypsin inhibitor were measured by mixing the equimolar concentration of the reactants in a Stopped - Flow apparatus at pH (4.5 to 10.0). The reaction of trypsin with soybean trypsin inhibitor was of first order with respect to the concentration of the reactants used. The rates of dissociation of the stable complexes, a-trypsin - soybean trypsin inhibitor, 13-trypsin - soybean trypsin inhibitor and p- trypsin - modified soybean trypsin inhibitor were also measured at pH (1.92 to 3.58). The values of first order rate constant, Ko obtained for the dissociation of all the three complexes were identical with one another. The kinetics results obtained for the porcine trypsin were compared with those of bovine trypsin system and it was suggested that the reaction mechanisms in both these systems were identical.
Page(s):
35-46
DOI:
DOI not available
Published:
Journal: Nucleus, Volume: 31, Issue: 1--4, Year: 1994