Roth G J, Machuga E T, Strittmatter P
J Biol Chem. 1981 Oct 10;256(19):10018-22.
Purified, apoprostaglandin synthetase was prepared from sheep vesicular gland and studied in terms of its heme-binding properties. The enzyme binds a single heme group per enzyme monomer, Mr = 70,000. When reconstituted with heme, the enzyme has an absorption maximum at 412 nm and an absorption coefficient, epsilon 412 nm, of 120 mM-1 cm-1. The binding of heme to the apoenzyme was accompanied by a proportional increase in enzyme activity up to the point of heme-binding saturation. This reconstituted holoenzyme forms prostaglandin H2 from arachidonate. We conclude that prostaglandin synthetase possesses the heme-binding properties of a "typical" heme protein and that a single heme group mediates both the oxygenase and the peroxidase activities of the enzyme.
从绵羊精囊制备了纯化的脱辅基前列腺素合成酶，并对其血红素结合特性进行了研究。该酶每个酶单体结合一个血红素基团，分子量为70,000。用血红素重构后，该酶在412nm处有最大吸收峰，吸收系数ε412nm为120mM-1cm-1。血红素与脱辅基酶的结合伴随着酶活性的成比例增加，直至血红素结合饱和点。这种重构的全酶由花生四烯酸形成前列腺素H2。我们得出结论，前列腺素合成酶具有“典型”血红素蛋白的血红素结合特性，并且单个血红素基团介导该酶的加氧酶和过氧化物酶活性。
