REACTIVATION BY DITHIOLS OF ENZYMES INHIBITED BY LEWISITE

REACTIVATION BY DITHIOLS OF ENZYMES INHIBITED BY LEWISITE
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DOI:
10.1042/bj0410069
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发表时间:
1947-01-01
影响因子:
4.1
通讯作者:
SINGER, TP
SINGER, TP
中科院分区:
生物学3区
文献类型:
--
作者:
BARRON, ESG;MILLER, ZB;SINGER, TP

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许多酶系统的蛋白质成分含有SH基团,它们要么是自由反应,要么是迟钝反应。自由反应的SH基团在中性蛋白质中进行硝普苷试验,容易被低浓度的轻度氧化剂和烷基化剂(醋酸碘、芥子气、双光气、氯化氰)氧化,并且容易形成巯基。在变性过程中,缓慢的SH基团变得自由作用。硫基干基酶分布广泛,存在于与蛋白质、脂肪和碳水化合物代谢有关的酶中。由于食物的代谢是通过一系列酶的反应来完成的,这些酶的反应在某些步骤上是相互联系的,因此,抑制巯基酶将对人体的代谢产生深远的干扰。过氧化剂或巯基形成剂对这些SH酶的抑制作用可以通过添加硫醇化合物来抵消。事实上,多年前Voegtlin, Dyer & Leonard (1923), Voegtlin, rosenthal&johnson(1931)和Eagle(1939)就成功地使用了硫醇来治疗动物砷中毒。然而,人们经常发现单硫醇是无效的。二硫醇的引入(Peters, Stocken & Thompson, 1945)标志着在氧化或巯基形成剂抑制的SH酶的再激活方面取得了重大进展,因此在这些物质引起的中毒治疗方面也取得了重大进展。
The protein component of a number of enzyme systems contains SH groups which are either freely reacting or sluggish. The freely reacting SH groups give the nitroprusside test in thenative protein, are easily oxidized by mild oxidizing agents and alkylating agents in low concentrations (iodoacetate, mustardgas, diphosgene, cyanogenchloride), and readily form mercaptides. On denaturation, the sluggish SH groups become freely acting. Sulphy-dryl enzymes are widely distributed, existing among the enzymes concerned with the metabolism of proteins, fats and carbohydrates. Since the meta-bolism of foodstuffs is performed by a series of enzymic reactions which in some steps are linked to each other, it follows that inhibition of sulphydryl enzymes will create profound disturbancesin the metabolism of the body. Inhibition ofany of these SH enzymes byoxidizing agents or mercaptide-forming agents can be counteracted by addition of thiol compounds. In fact, thiols were used success-fully years ago by Voegtlin, Dyer & Leonard (1923), Voegtlin, Rosenthal& Johnson (1931), and by Eagle (1939), in the treatment of arsenical poisoning in animals. Monothiols, however, were often found inefficacious. The introduction of dithiols (Peters, Stocken & Thompson, 1945) has marked a great progress in the reactivation of SH enzymes inhibited by oxidizing or mercaptide-forming agents, and hence in the treatment of intoxications produced by these substances.