title: Kinetics of thermal inactivation of penaeus penicillatus acid phosphatase
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.
authors.affiliation: Department of Biology, Xiamen University, Xiamen, 361005, People's Republic of China.
authors.initials: P
authors.lastname: Yang
authors.initials: Q
authors.lastname: Chen
authors.initials: Z
authors.lastname: Xie
authors.initials: S
authors.lastname: Chen
authors.initials: Y
authors.lastname: Yang
authors.initials: Y
authors.lastname: Park
authors.initials: H
authors.lastname: Zhou