PMID: 6968591Oct 14, 1980Paper

Interaction of chymotrypsinogens with alpha 1-protease inhibitor

Biochemistry
J W BrodrickH Maeda

Abstract

In a previous report [Largman, C., Brodrick, J.W., Geokas, M.C., Sischo, W.M., & Johnson, J.H. (1979) J. Biol. Chem. 254, 8516-8523] it was demonstrated that human proelastase 2 and alpha 1-protease inhibitor react slowly to form a complex that is stable to denaturation with sodium dodecyl sulfate and beta-mercaptoethanol and that the zymogen can be recovered from the isolated complex following dissociation by hydroxylamine. The present report demonstrates that bovine chymotrypsinogen A reacts with human alpha 1-protease inhibitor in a very similar manner. The rate of complex formation was measured by two methods. In the first, the reaction was followed by determining the loss of the inhibitory activity of alpha 1-protease inhibitor as a function of time. A second-order rate constant for complex formation formation (pH 7.6, 36 degrees C) of 12.9 +/- 2.4 M-1s-1 was obtained. In the second procedure, the reaction of fluorescein isothiocyanate labeled chymotrypsinogen A with alpha 1-protease inhibitor was measured by fluorescence polarization. A second-order rate constant (pH 7.6, 37 degrees C) of 13.9 +/- 2.1 M-1s-1 was obtained. The rate of complex formation is approximately 10(-5) of that measured for the reaction of bovine chy...Continue Reading

References

Nov 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·P H MorganH Neurath
Feb 5, 1980·Biochemistry·E G Del MarM C Geokas

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Citations

Jun 1, 1989·Analytical Biochemistry·V E DuffyB C Monk
Oct 1, 1981·International Journal of Peptide and Protein Research·L Karic, C B Glaser
Feb 10, 1995·Cancer Letters·A S Varela, J J López Sáez
Nov 15, 1984·Analytical Biochemistry·S S Twining
Feb 1, 1992·International Journal of Pancreatology : Official Journal of the International Association of Pancreatology·S HayakawaS Naruse

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