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Simultaneous analysis of catechol‐ O ‐methyl transferase activity, S ‐adenosylhomocysteine and adenosine
Author(s) -
Reenilä Ilkka,
Rauhala Pekka
Publication year - 2010
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.1288
Subject(s) - chemistry , catechol o methyl transferase , entacapone , catechol , methyltransferase , chromatography , vanillic acid , biochemistry , adenosine , incubation , transferase , high performance liquid chromatography , enzyme , methylation , levodopa , medicine , allele , disease , parkinson's disease , gene
Novel HPLC method utilizing UV‐detection was developed to analyse catechol‐ O ‐methyltransferase (COMT) products, vanillic acid and isovanillic acid, S ‐adenosylhomocysteine (SAH) and adenosine formed from dihydroxybenzoic acid and S ‐adenosyl‐L‐methionine (SAM) by incubation of the rat tissues. Entacapone, a COMT inhibitor, prevented the formation of SAH only partially in the striatal homogenate whereas in the kidney homogenate the increase of SAH was prevented by entacapone. In conclusion, this method was reliable, rapid and simple. COMT seemed to be partially responsible on the SAM utilizing methylations in the striatal homogenates while in the high COMT activity tissue, COMT was the main SAH producing methyltransferase. Copyright © 2009 John Wiley & Sons, Ltd.