Acid phosphatase (E.C.3.1.3.2.) thermal deactivation at pH 3.77 has been investigated by monitoring the enzyme activity as a function of time in the hydrolysis of p‐nitrophenyl phosphate. The experimental curves obtained show a two‐slope behavior in a log (activity)versus‐time plot, which indicates that deactivation occurs via a complex mechanism. From the dependence of the kinetic parameters on both deactivation and hydrolysis temperatures, it is inferred that the deactivation mechanism involves intermediate, temperature‐dependent, less‐active forms of the enzy
Acid phosphatase deactivation by a series mechanism / Gianfreda, Liliana; Marrucci, Giuseppe; Grizzuti, Nino; Greco, Guido. - In: BIOTECHNOLOGY AND BIOENGINEERING. - ISSN 0006-3592. - STAMPA. - 26:5(1984), pp. 518-527. [10.1002/bit.260260518]
Acid phosphatase deactivation by a series mechanism
GIANFREDA, LILIANA;MARRUCCI, GIUSEPPE;GRIZZUTI, NINO;GRECO, GUIDO
1984
Abstract
Acid phosphatase (E.C.3.1.3.2.) thermal deactivation at pH 3.77 has been investigated by monitoring the enzyme activity as a function of time in the hydrolysis of p‐nitrophenyl phosphate. The experimental curves obtained show a two‐slope behavior in a log (activity)versus‐time plot, which indicates that deactivation occurs via a complex mechanism. From the dependence of the kinetic parameters on both deactivation and hydrolysis temperatures, it is inferred that the deactivation mechanism involves intermediate, temperature‐dependent, less‐active forms of the enzyI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
