Premium
Spectrofluorimetric Quantification of Malondialdehyde for Evaluation of Cyclooxygenase‐1/Thromboxane Synthase Inhibition
Author(s) -
Dannhardt Gerd,
Flemmer Linda,
Hartmann Rolf W.,
Kleber Alice,
Schulze Elfriede
Publication year - 1998
Publication title -
archiv der pharmazie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 61
eISSN - 1521-4184
pISSN - 0365-6233
DOI - 10.1002/(sici)1521-4184(199811)331:11<359::aid-ardp359>3.0.co;2-b
Subject(s) - chemistry , cyclooxygenase , malondialdehyde , thromboxane a synthase , arachidonic acid , thromboxane , eicosanoid , biochemistry , atp synthase , thromboxane b2 , whole blood , thiobarbituric acid , pharmacology , chromatography , platelet , enzyme , lipid peroxidation , oxidative stress , medicine
The in vitro assay developed by Hartmann and Ledergerber (1995) [1] utilizing the Spectrofluorimetric quantification of malondialdehyde after reaction with thiobarbituric acid was modified and used for further investigations. The human whole blood was replaced by a platelet suspension of pig blood, and calcium ionophore A23187 was used instead of collagen for inducing the arachidonic acid cascade. The modified assay represents a simple, time and cost saving method for the evaluation of cyclooxygenase‐1/thromboxane synthase inhibition. The reproducibility and comparability of results is given. Additional experiments allow classification of selective phospholipase A 2 , cyclooxygenase‐1, and thromboxane synthase inhibitors. Further studies of malondialdehyde formation show that the cyclooxygenase and/or the thromboxane synthase are competitively inhibited by reaction products of the cyclooxygenase pathway by a negative feedback mechanism.