Download Biochemistry of Arachidonic Acid Metabolism by Richard J. Kulmacz (auth.), Dr. William E. M. Lands (eds.) PDF
By Richard J. Kulmacz (auth.), Dr. William E. M. Lands (eds.)
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Extra info for Biochemistry of Arachidonic Acid Metabolism
Biochem. Biophys. Res. Comm. (95): 103-110, 1980. 62. Lands WEM, Cook HW, Rome LH: Prostaglandin biosynthesis: Consequences of oxygenase mechanism upon in vitro assays of drug effectiveness. In: Samuelsson, B, Paoletfi~(eds) Advances in Prostaglandin an~Thromboxane Research Vol. 1. Raven Press, New York, 1976, pp 7-17. 63. Lands WEM, Hanel AM: Inhibitors and activators of prostaglandin biosynthesis. In: Pace-Asciak, C, Granstrom, E (eds) Prostaglandins and related substances. Elsevier, Amsterdam, 1983, pp 203-223.
Chern. (250): 1765-70, 1975. 76. Galpin JR, Teilens AGM, Veldink GA, Vliegenthart JFG, Boldingh J: On the interaction of some catechol derivatives with the iron atom of soybean lipoxygenase. FEBS Lett. (69): 179-82, 1976; Spaapen, LJM, Verhagen J, Veldink GA, Vliegenthart JFG: Properties of a complex of Fe(III)-soybean lipoxygenase-1 and 4-nitrocatechol. Biochim. Biophys. Acta (617): 132-140, 1980. 77. Vanderhoek JY, Lands WEM: Evidence for H202 mediating the irreversible action of acetylenic inhibitors of prostaglandin biosynthesis.
When the 5-hydroxyl group was modified to a methoxyl group, inhibitory potency decreased approximately 4-fold and converting the 3' and 4' hydroxyl groups to methoxyl groups virtually eliminated all inhibitory potency. 4 ~M. Again, the phenolic structure strongly suggests that these derivatives might function as antioxidants. 3. This unexplained reaction of the catechol was regarded to be virtually stoichiometric and apparently irreversible (76). Further study indicated that an initial reversible inhibition of lipoxygenase by this catechol could shift slowly to an irreversible inactivation (76) by 25 interaction with the hydroperoxide-enzyme complex although it did not do so with the native lipoxygenase alone.