Fylling A C, Westlund P, Helander A
Department of Woman and Child Health, Karolinska Hospital, Stockholm, Sweden.
Prostaglandins. 1995 Nov-Dec;50(5-6):287-99. doi: 10.1016/0090-6980(95)00130-1.
We have recently purified 11-hydroxythromboxane B2 dehydrogenase from porcine kidney and identified it as cytosolic aldehyde dehydrogenase (EC 1.2.1.3) based on amino acid analysis and other protein characteristics. In the present paper we have studied the catalytic interaction of thromboxane B2 (TXB2) with different aldehyde substrates and a potent aldehyde dehydrogenase inhibitor, disulfiram. TXB2 was a competitive inhibitor of the aldehyde dehydrogenase reaction in assays with 3,4-dihydroxyphenylacetaldehyde, a high affinity substrate. The conversion of TXB2 to 11-dehydro-TXB2 was also inhibited by propanal and disulfiram. The protein characteristics of the enzyme have also been further studied. The native enzyme is a tetramer and has an isoelectric point of 7.0 which is comparable with that of cytosolic aldehyde dehydrogenases from other species. Taken together the present data further indicate that 11-hydroxythromboxane B2 dehydrogenase is identical with cytosolic aldehyde dehydrogenase and that substrates and inhibitors of aldehyde dehydrogenase interact with thromboxane metabolism in vitro.
我们最近从猪肾中纯化了11-羟基血栓素B2脱氢酶，并根据氨基酸分析和其他蛋白质特性将其鉴定为胞质醛脱氢酶（EC 1.2.1.3）。在本文中，我们研究了血栓素B2（TXB2）与不同醛底物以及一种有效的醛脱氢酶抑制剂双硫仑之间的催化相互作用。在以高亲和力底物3,4-二羟基苯乙醛进行的测定中，TXB2是醛脱氢酶反应的竞争性抑制剂。丙醛和双硫仑也抑制TXB2向11-脱氢-TXB2的转化。我们还进一步研究了该酶的蛋白质特性。天然酶是一种四聚体，其等电点为7.0，这与其他物种的胞质醛脱氢酶相当。综上所述，目前的数据进一步表明11-羟基血栓素B2脱氢酶与胞质醛脱氢酶相同，并且醛脱氢酶的底物和抑制剂在体外与血栓素代谢相互作用。
