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
中科院分区:
文献类型:
--
作者:
BARRON, ESG;MILLER, ZB;SINGER, TP
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.