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- Title
Human Urinary Proteinase Inhibitor: Inhibitory Properties and Interaction with Bovine Trypsin.
- Authors
BALDUYCK, Malika; DAVRIL, Monique; MIZON, Charlotte; SMYRLAKI, Marie; HAYEM, Annette; MIZON, Jacques
- Abstract
The major urinary trypsin inhibitor (UTI) was found to inhibit bovine chymotrypsin and human leucocyte elastase strongly, cathepsin G weakly. No inhibition of porcine pancreatic elastase was observed. The stoichiometry of the inhibition of bovine trypsin by UTI was determined spectrophotometrically to be 1:2 (I/E molar ratio). After incubation of UTI with this enzyme in various molar ratios, two complexes (C1 and C2) could be visualized in alkaline polyacrylamide gel electrophoresis. C1 was isolated by affinity chromatography on Con- Sepharose. In dodecyl sulfate polyacrylamide gel electrophoresis, C1 was dissociated to give an inhibitory band with the same electrophoretic mobility as native UTI. C2 released an active inhibitory fragment with Mr near 20000. A time-course study demonstrated that at a molar ratio I/E of 1.5:1, the C2 complex appears after two hours of incubation.
- Publication
Biological Chemistry, 1985, Vol 366, Issue 1, p9
- ISSN
1431-6730
- Publication type
Article