首页> 外文期刊>Ukrainian Biochemical Journal >Coordinative compounds of zinc with N-substituted thiоcаrbаmоil-N′-pentаmethylеnsulfenаmides – activity mоdifiers of еnzymes of proteolytic and glycolytic action
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Coordinative compounds of zinc with N-substituted thiоcаrbаmоil-N′-pentаmethylеnsulfenаmides – activity mоdifiers of еnzymes of proteolytic and glycolytic action

机译:锌与N-取代的噻吩甲基-N'-五甲基甲基亚磺酰胺的配位化合物-蛋白水解和糖酵解酶活性的调节剂

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The influence of a number of coordinative compounds of zinc with N-substituted thiocarbamoil-N′-pentamethylensulfenamides on activity of elastase, α-L-rhamnosidase and α-galactosidases evidence for a possibility of their usage as stimulators or inhibitors of enzymes tested have been studied. It was shown that all the compounds in concentration of 0.1 and 0.01% inhibited by 90–100% Bacillus thuringiensis 27-88Elssup+/sup elastase activity. [Zn(Lsub2/sub)Brsub2/sub], [Zn(Lsub1/sub)(NCS)sub2/sub] and [Zn(Lsub3/sub)(NCS)sub2/sub] at 20 h exposition activated Cryptococcus albidus 1001 α-L-rhamnosidase activity. The rest of compounds influenced it on the control level or inhibited it by 7–23%. The obtained results testify that essential role is not played by separate fragments (L-ligand and anions), but by molecules of zinc complexes as a whole. All the studied complexes, exept for [Zn(Lsub3/sub)(NCS)sub2/sub], induced α-L-rhamnosidase activity of Еupenicillium erubescens 248 (7 to 60%). All zinc compounds (concentration 0.01%, exposition time – 60 min) influenced at the control level Aspergillus niger and Cladosporium cladosporioides α-galactosidases activity, however inhibited (up to 20%) activity of Penicillium canescens α-galactosidase. The increasing of exposition time of the compounds tested with enzymes up to 20 h testify to selective action of separate compounds on enzymes tested. The data obtained prove, that the character of interaction of zinc complexes is changed depending on the enzyme tested and its strain-producer.
机译:锌与N-取代的硫代氨基甲酸酯-N'-五甲基亚磺酰胺的许多配位化合物对弹性蛋白酶,α-L-鼠李糖苷酶和α-半乳糖苷酶活性的影响已证明它们可能用作测试酶的刺激剂或抑制剂研究。结果表明,所有浓度为0.1%和0.01%的化合物均受到90–100%苏云金芽孢杆菌27-88Els + 弹性蛋白酶活性的抑制。 [Zn(L 2 )Br 2 ],[Zn(L 1 )(NCS) 2 ]和[Zn(L 3 )(NCS) 2 ]在20 h暴露后激活了隐隐隐球菌1001α-L-鼠李糖苷酶活性。其余化合物在控制水平上影响它或将其抑制7-23%。获得的结果证明,重要的作用不是由单独的片段(L-配体和阴离子)发挥作用,而是锌配合物的整体分子发挥了作用。除[Zn(L 3 )(NCS) 2 ]外,所有已研究的复合物均诱导了淡色细小球菌248的α-L-鼠李糖苷酶活性(7%至60%) 。所有的锌化合物(浓度为0.01%,暴露时间为60分钟)均在对照水平上影响了黑曲霉和克氏梭状芽孢杆菌α-半乳糖苷酶的活性,但抑制了蔗糖青霉α-半乳糖苷酶的活性(高达20%)。用酶测试的化合物暴露时间最多增加20小时,这证明了单独的化合物对测试酶的选择性作用。所获得的数据证明,锌配合物相互作用的特性根据所测试的酶及其菌株产生者而改变。

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