1981
DOI: 10.1016/s0378-4347(00)86081-8
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Assay of catechol O-methyltransferase activity by high-performance liquid chromatography with electrochemical detection

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Cited by 17 publications
(2 citation statements)
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“…From the metabolic point of view, position 3 can be assumed, as methylation of the catechol metabolite to the corresponding hydroxymethoxy metabolite should be catalyzed by catechol‐ O ‐methyltransferase (COMT). This enzyme is known to have a higher preference for this position 27–30. The identity of 3,4‐methylenedioxybenzylamine and piperazine could be confirmed by comparing their mass spectra and GC retention times with those of their reference substances.…”
Section: Resultsmentioning
confidence: 88%
“…From the metabolic point of view, position 3 can be assumed, as methylation of the catechol metabolite to the corresponding hydroxymethoxy metabolite should be catalyzed by catechol‐ O ‐methyltransferase (COMT). This enzyme is known to have a higher preference for this position 27–30. The identity of 3,4‐methylenedioxybenzylamine and piperazine could be confirmed by comparing their mass spectra and GC retention times with those of their reference substances.…”
Section: Resultsmentioning
confidence: 88%
“…For this purpose, a number of different compounds have been used as a substrate for COMT including naturally including catechols (Zurcher and Da Prada, 1982) (Nohta et al, 1984) and DHBA (Koh et al, 1981;Nissinen and Mannisto, 1984;Schultz et al, 1989;Smit et al, 1990). However, the use of several of these substrates presents some limitations in measuring COMT activity.…”
Section: Discussionmentioning
confidence: 99%