Premium
Rat liver and kidney catechol‐ O ‐methyltransferase activity measured by high‐performance liquid chromatography with fluorescence detection
Author(s) -
Tsunoda Makoto,
Takezawa Kazuko,
Masuda Mayumi,
Imai Kazuhiro
Publication year - 2002
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.202
Subject(s) - catechol o methyl transferase , chemistry , catechol , chromatography , high performance liquid chromatography , kidney , fluorescence , substrate (aquarium) , endogeny , enzyme , biochemistry , yield (engineering) , endocrinology , biology , ecology , allele , physics , quantum mechanics , gene , materials science , metallurgy
We have previously reported a highly sensitive method for the measurement of catechol‐ O ‐methyltransferase (COMT) activities in rat erythrocytes with norepinephrine (NE), an endogenous native substrate, using high‐performance liquid chromatography (HPLC)‐fluorescence or peroxyoxalate chemiluminescence reaction detection. Applying this method to COMT activities in rat liver and kidney, known to have the highest activities of all organs, the optimum reaction conditions were investigated. Under the optimum conditions, soluble (S)‐COMT and membrane‐bound (MB)‐COMT activities in rat liver, with NE as a substrate, were 2.17 ± 0.33 and 0.16 ± 0.02 nmol/min/mg protein ( n = 5), respectively. In rat kidney, S‐COMT and MB‐COMT activities were 1.81 ± 0.20 and 0.079 ± 0.009 nmol/min/mg protein ( n = 5), respectively. Since liver and kidney play important roles in inactivating catecholamines, using the proposed method would yield critical information to delineate the role of metabolism of catecholamines in rat tissues. Copyright © 2002 John Wiley & Sons, Ltd.