V. Simeon et E. Pavkovic, HEAT INACTIVATION OF PARAOXONASE AND ARYLESTERASE ACTIVITIES IN HUMANAND RABBIT SERUM, Chemico-biological interactions, 87(1-3), 1993, pp. 103-107
The heat inactivation of esterases in human and rabbit serum was follo
wed at 50 and 55-degrees-C by measuring the decrease of activity with
paraoxon, phenylacetate and beta-naphthylacetate as substrates. The ra
te of inactivation measured with the three substrates was slightly, bu
t significantly different, indicating that the substrates are hydrolys
ed by different enzymes.