Activity of cholinesterases in human whole blood measured with acetylthiocholine as substrate and ethopropazine as selective inhibitor of plasma butyrylcholinesterase.

نویسندگان

  • Elsa Reiner
  • Anita Bosak
  • Vera Simeon-Rudolf
چکیده

A procedure is suggested for measuring acetylcholinesterase and butyrylcholinesterase activities in human whole blood using acetylthiocholine as a substrate and ethopropazine as a selective inhibitor of butyrylcholinesterase. The procedure is suitable for screening cholinesterase activities in routine and/or field tests.

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منابع مشابه

A New Assay for Measurement of Acetylcholinesterase and Butyrylcholinesterase in Canine Whole Blood Combining Specific Substrates and Ethopropazine Hydrochloride as a Selective Butyrylcholinesterase Inhibitor

Received: Revised: Accepted: April 13, 2013 April 17, 2013 April 24, 2013 In the present report, a new assay combining specific substrates and a selective BChE inhibitor (ethopropazine hydrochloride) was used to measure both AChE and BChE in canine whole blood samples. Acetylthiocholine iodide (ATCI) and butyrylthiocholine iodide (BTCI) were used as substrates, whereas 2,2’dithiodipiridine was ...

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Species variation in the specificity of cholinesterases in human and rat blood samples.

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Kinetics of hydrolysis of acetylcholine and acetylthiocholine by two types of acetylcholinesterase and butyrylcholinesterase inhibited by 13 new inhibitors (5 carbamates and 8 carbazates--hydrazinium derivatives) was measured in vitro in a batch reactor at 25 degrees C, pH 8, ionic strength 0.11 M and enzyme activity 3.5 U by four nondependent analytical methods. Sevin, rivastigmin (Exelon) and...

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عنوان ژورنال:
  • Arhiv za higijenu rada i toksikologiju

دوره 55 1  شماره 

صفحات  -

تاریخ انتشار 2004