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ACTION OF TRIBUTYLTIN ON ENZYMES OF FOUR BACTERIA

机译:三丁基锡对四种细菌酶的作用

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The effect of tributyltin (TBT) was examined on six enzymes in intact cells and in cytosol and wall/membrane fractions of four bacteria. The organisms' TBT resistance varied over 2,400-fold: Pseudomonas putida TBT-6 > Pseudomonas sp. BP-4 > Bacillus sp. Me-Ⅰ > Bacillus sp. MC-24S. TBT is not a general toxicant for enzymes since β-galactosidase, glucose de-hydrogenase, and alkaline phosphatase were not affected by it. ATPase was detected in cells of all four organisms but not in their cell fractions; it Was inhibited by TBT in cells of Bacillus sp. MC-24S. In intact cells and the membrane fraction, TBT stimulated NADH oxidase at low levels and inhibited it at higher levels, and the more resistant organisms had a higher threshold concentration. In Pseudomonas sp. BP-4, TBT had no effect on glucose-6-phosphate dehydrogenase in cells, but inhibited it in the cytosol fraction. TBT did not affect the periplasmic alkaline phosphatase, which was present in the two Pseudomonas spp. The results support the conclusion that the cell membrane is a site of action of TBT, but that it can also act in the cytoplasm, for the cytosolic enzyme glucose-6-phosphate dehydrogenase was stimulated in cells of Bacillus sp. MC-24S. Enzymes requiring free sulfhydryl groups were inhibited. The patterns of enzyme sensitivity to TBT suggest there may be two resistance mechanisms among these four organisms.
机译:检查了三丁基锡(TBT)对完整细胞中以及四种细菌的细胞溶质和壁/膜级分中的六种酶的影响。生物体的TBT抵抗力变化超过2,400倍:恶臭假单胞菌TBT-6>假单胞菌。 BP-4>芽孢杆菌Me-Ⅰ>芽孢杆菌MC-24S。 TBT不是酶的一般毒物,因为β-半乳糖苷酶,葡萄糖脱氢酶和碱性磷酸酶不受其影响。在所有四种生物的细胞中均检测到ATPase,但在其细胞级分中未检测到;它被芽孢杆菌属细胞中的TBT抑制。 MC-24S。在完整的细胞和膜级分中,TBT可以低水平刺激NADH氧化酶,而在较高水平则可以抑制NADH氧化酶,而耐药性更高的生物具有较高的阈值浓度。在假单胞菌中。 BP-4,TBT对细胞中的6-6磷酸葡萄糖脱氢酶没有影响,但在细胞溶质中抑制了它。 TBT不会影响周质碱性磷酸酶,这存在于两个假单胞菌属物种中。该结果支持这样的结论,即细胞膜是TBT的作用位点,但它也可以在细胞质中起作用,因为在芽孢杆菌属的细胞中刺激了胞质酶葡萄糖-6-磷酸脱氢酶。 MC-24S。需要游离巯基的酶被抑制。酶对TBT的敏感性模式表明,这四种生物之间可能存在两种抗药性机制。

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