1999•PubMedRequires access
Kinetics of thermal inactivation of penaeus penicillatus acid phosphatase
Pei‐Zheng Yang, Q.-X. Chen, Zhaoxiong Xie, S.-L. Chen, Yi Yang, Y.-D. Park, Hai‐Meng Zhou
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Abstract
The kinetics of thermal inactivation of Penaeus penicillatus acid phosphatase have been studied using a kinetic method related to the substrate reaction during irreversible inhibition of the enzyme activity as previously described by Tsou (Adv. Enzymol. Relat. Areas Mol. Biol. (1988) 61, 381-436). The kinetics of thermal inactivation of the enzyme show that the reaction is irreversible. The microscopic rate constants were determined for thermal inactivation of free enzyme and the enzyme--substrate complex. The results show that the presence of substrate has a significant protective effect against thermal inactivation of the enzyme.