Ogino N, Miyamoto T, Yamamoto S, Hayaishi O
J Biol Chem. 1977 Feb 10;252(3):890-5.
Prostaglandin endoperoxide E isomerase catalyzes the isomerization of the endoperoxy group of prostaglandin H and produces prostaglandin E. The enzyme was solubilized with Tween 20 from bovine vesicular gland microsomes and purified 26-fold by successive column chromatography on DEAE-cellulose and omega-aminobutyl Sepharose 4B. The previously known requirement for glutathione was further investigated. The activity of freshly prepared enzyme was destroyed rapidly with a half-life of about 30 min at 24 degrees, pH 8.0. Various thiol compounds including glutathione protected the enzyme from such an inactivation. However, several findings indicated that glutathione was possibly specifically involved as a coenzyme in the isomerase reaction, but was not oxidized in a stoichiometric quantity. The enzyme also isomerized prostaglandin G at a rate approximately half of that of prostaglandin H.
前列腺素内过氧化物E异构酶催化前列腺素H内过氧基团的异构化反应,生成前列腺素E。该酶用吐温20从牛精囊微粒体中溶解出来,并通过先后在DEAE - 纤维素和ω-氨基丁基琼脂糖4B柱上进行层析,纯化了26倍。对先前已知的谷胱甘肽需求进行了进一步研究。新制备的酶的活性在24℃、pH 8.0条件下迅速丧失,半衰期约为30分钟。包括谷胱甘肽在内的各种硫醇化合物可保护该酶不被这种失活作用影响。然而,多项研究结果表明,谷胱甘肽可能作为辅酶特异性地参与异构酶反应,但并非以化学计量的量被氧化。该酶异构化前列腺素G的速率约为前列腺素H的一半。