2310525 |
Coletta M, Ascenzi P, Bravin L, Amiconi G, Bolognesi M, Guarneri M, Menegatti E: Thermodynamic modeling of internal equilibria involved in the activation of trypsinogen. J Biomol Struct Dyn. 1990 Feb;7(4):959-72.
The effect of activating dipeptides, sequentially homologous to the Ile16-Val17N-terminus of bovine beta-trypsin (beta-trypsin), on equilibria involved in the binding of strong ligands (i.e., n-butylamine, the bovine basic pancreatic trypsin inhibitor (Kunitz-type inhibitor; BPTI) and the porcine pancreatic secretory trypsin inhibitor (Kazal-type inhibitor, type I; PSTI)) to bovine trypsinogen (trypsinogen) was investigated at pH 5.51 (I = 0.1 M) and T = 21.0 +/- 0.5 degrees C; under the same experimental conditions, thermodynamics for the binding of strong ligands to beta-trypsin was also obtained. |
162(2,2,2,2) |
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2285797 |
Coletta M, Ascenzi P, Amiconi G, Bolognesi M, Guarneri M, Menegatti E: Bovine trypsinogen activation. Biophys Chem. 1990 Aug 31;37(1-3):355-62.
The N-alpha-L-isoleucyl-L-valine (Ile-Val) activating dipeptide, sequentially homologous to the Ile 16-Val 17 N-terminus of bovine beta-trypsin, displays an activating effect on equilibria involved in the binding of strong ligands (i.e., n-butylamine and the porcine pancreatic secretory trypsin inhibitor (Kazal-type inhibitor, type I; PSTI)) to bovine trypsinogen. |
81(1,1,1,1) |
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