Heat inactivation of paraoxonase and arylesterase activities in human and rabbit serum.
The heat inactivation of esterases in human and rabbit serum was followed at 50 and 55 degrees C by measuring the decrease of activity with paraoxon, phenylacetate and beta-naphthylacetate as substrates. The rate of inactivation measured with the three substrates was slightly, but significantly different, indicating that the substrates are hydrolysed by different enzymes.
Simeon
V
V
Institute for Medical Research and Occupational Health, University of Zagreb, Croatia.
Pavković
E
E
D000818:Animals; D043303:Aryldialkylphosphatase; D002265:Carboxylic Ester Hydrolases / Q000097:blood*; D004347:Drug Interactions; D004789:Enzyme Activation; D004795:Enzyme Stability; D006358:Hot Temperature; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D009280:Naphthaleneacetic Acids / Q000097:blood; D010261:Paraoxon / Q000097:blood; D010648:Phenylacetates / Q000097:blood; D010744:Phosphoric Monoester Hydrolases / Q000097:blood*; D011817:Rabbits
D009280:Naphthaleneacetic Acids; D010648:Phenylacetates; C020424:2-naphthylacetic acid; D002265:Carboxylic Ester Hydrolases; C019734:arylesterase; D010744:Phosphoric Monoester Hydrolases; D043303:Aryldialkylphosphatase; C025136:phenylacetic acid; D010261:Paraoxon