The thermal stability of bovine tryptase, a serine proteinase present in the bovine mast cell secretory granules, has been studied by circular dichroism and catalytic activity measurements. Bovine tryptase shows a peculiar dichroic negative band centered at 230 nm. The decrease of this band in a temperature dependent fashion represents a good marker to monitor the native conformation of the enzyme. Bovine tryptase inactivation has been followed in the temperature range between 10 degrees C and 80 degrees C, and reversibility of the process has been also studied. The results obtained show that the temperature dependent loss of activity and the conformational change, as monitored by circular dichroism, are both fully reversible between 10 degrees C and 40 degrees C, while only the CD change displays reversibility in going from 60 degrees C to 10 degrees C. Moreover, a functional analysis of the temperature-dependent enzymatic activity of bovine tryptase toward peptide substrates in the 10 degrees C-40 degrees C range is reported and compared with the temperature dependence of the enzymatic activity of trypsin. (C) 1998 Elsevier Science Inc.

Erba, F., Fiorucci, L., Coletta, M., ASCOLI MARCHETTI, F. (1998). Bovine mast cell tryptase inactivation: Effect of temperature. PEPTIDES, 19(3), 437-443 [10.1016/S0196-9781(97)00423-3].

Bovine mast cell tryptase inactivation: Effect of temperature

ERBA, FULVIO;FIORUCCI, LAURA;COLETTA, MASSIMILIANO;ASCOLI MARCHETTI, FRANCA
1998

Abstract

The thermal stability of bovine tryptase, a serine proteinase present in the bovine mast cell secretory granules, has been studied by circular dichroism and catalytic activity measurements. Bovine tryptase shows a peculiar dichroic negative band centered at 230 nm. The decrease of this band in a temperature dependent fashion represents a good marker to monitor the native conformation of the enzyme. Bovine tryptase inactivation has been followed in the temperature range between 10 degrees C and 80 degrees C, and reversibility of the process has been also studied. The results obtained show that the temperature dependent loss of activity and the conformational change, as monitored by circular dichroism, are both fully reversible between 10 degrees C and 40 degrees C, while only the CD change displays reversibility in going from 60 degrees C to 10 degrees C. Moreover, a functional analysis of the temperature-dependent enzymatic activity of bovine tryptase toward peptide substrates in the 10 degrees C-40 degrees C range is reported and compared with the temperature dependence of the enzymatic activity of trypsin. (C) 1998 Elsevier Science Inc.
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10
English
Con Impact Factor ISI
Bovine tryptase; Catalytic activity; Circular dichroism; Energy parameters; Mast cells; Thermodynamic parameters
Erba, F., Fiorucci, L., Coletta, M., ASCOLI MARCHETTI, F. (1998). Bovine mast cell tryptase inactivation: Effect of temperature. PEPTIDES, 19(3), 437-443 [10.1016/S0196-9781(97)00423-3].
Erba, F; Fiorucci, L; Coletta, M; ASCOLI MARCHETTI, F
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/52604
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