Gel filtration and disc electrophoresis were used as simple and fast techniques for the investigation of the interaction and stoichiometry between UTI and trypsin. UTI appears to possess only a single trypsin binding site. The nature of the interaction between the inhibitor and enzyme appears to be dependent on the concentration ratio of the reactants. When UTI is in excess molar concentration, a single binary complex with trypsin of mol. wt. 95,000 is observed. In the presence of a molar excess of enzyme, this macromolecule is no longer observed, but proteins of mol. wt. 41,000 and 20,000 result. The possibility that UTI may be hydrolyzed to a partially degraded active fragment by the excess enzyme resulting in the formation of a modified inhibitor enzyme complex is proposed.
Proceedings of the Iowa Academy of Science
© Copyright 1973 by the Iowa Academy of Science, Inc.
Proksch, G. J. and Routh, J. I.
"The Interaction Between the Urinary Trypsin Inhibitor and Trypsin,"
Proceedings of the Iowa Academy of Science: Vol. 80:
, Article 5.
Available at: http://scholarworks.uni.edu/pias/vol80/iss2/5