Acid phosphatase deactivation by a series mechanism.
Biotechnol Bioeng
; 26(5): 518-27, 1984 May.
Article
in En
| MEDLINE
| ID: mdl-18553349
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 enzyme. This interpretation is confirmed by the results of additional tests in which the temperature was suddenly changed during the deactivation process.
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Collection:
01-internacional
Database:
MEDLINE
Language:
En
Journal:
Biotechnol Bioeng
Year:
1984
Document type:
Article
Affiliation country: