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.
Institute for Medical Research and Occupational Health, University of Zagreb, Croatia.
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Simeon
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Pavković
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