動物組織のリポキシゲナーゼの研究 : I.酵素の精製とその反応機構

概要

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Monoclonal antibodies were raised against arachidonate 12- and 5-lipoxy-genases of porcine leukocytes using partially purified enzyme as antigen. The two lipoxygenases were highly purified by immunoaffinity chromatography utilizing the anti-lipoxygenase antibodies. Studies with the purified enzymes demonstrated their multi-functional catalytic properties. In addition to 12-oxygenation of arachidonic acid, the purified 12-lipoxygenase catalyzed 8S- and 14R-oxy-genation and 14,15-epoxidation of 15-hydroperoxyeicosatetraenoic acid. 5-Lipoxygenase showed both arachidonate 5-oxygenation and 5,6-epoxidation of 5-hydroperoxy acid (leukotriene A_4 Synthesis). Lipoxin synthesis from 5,15-dihydroperoxy acid was demonstrated with both 12- and 5-lipoxygenases.
日本ビタミン学会の論文
1988-01-25