Search results for "Pentachlorophenol"
showing 3 items of 23 documents
Effects of Pentachlorophenol and Biotic Interactions on Soil Fauna and Decomposition in Humus Soil
1995
In a laboratory experiment, effects of chemical stress (pentachlorophenol, PCP, at concentrations of 0, 50, and 500 mg/kg) and biotic interactions (nematodes in the presence or absence of collembolas and enchytraeids) on the community structure of soil animals and decomposition processes were studied. PCP was strongly adsorbed to humus that contained 65% organic matter. Numbers of fungal-feeding nematodes decreased significantly at the highest PCP concentration, while no effects were found in bacterial feeders. There were differences in the numbers of nematodes between different animal combinations, but at the highest PCP concentration, collembolas and enchytraeids had no effect on them. Nu…
Responses of two earthworm populations with different exposure histories to chlorophenol contamination
1998
Two populations of the earthworm Aporrectodea tuberculata (Eisen), one from a chlorophenol contaminated and another from an uncontaminated site in central Finland, were exposed to acute, toxic, and sublethal concentrations of pentachlorophenol (PCP). Exposure history seemed to have only slight effect on the responses of the earthworms. Values of a lethal concentration of 50% in the humus-rich soil were very high, 1,870 μg PCP per gram for the earthworms from the contaminated site and 1,520 μg/g for the earthworms from the uncontaminated site. No differences in the accumulation of PCP from the soil into the earthworms between the two populations were found. Earthworms from both populations s…
Production and characterization of the recombinant Sphingomonas chlorophenolica pentachlorophenol 4-monooxygenase.
2001
Abstract Pentachlorophenol 4-monooxygenase (PCP4MO) from Sphingomonas chlorophenolica is a flavoprotein that hydroxylates PCP in the presence of NADPH and oxygen. In order to investigate the structure and function of active site, recombinant PCP4MO (rePCP4MO) was produced in Escherichia coli as a glutathione S-transferase (GST) fusion protein. Moreover, a tobacco etch virus (TEV) protease cleavage site (EKLYFQG) was introduced into GST-PCP4MO and a his-tagged TEV protease was employed. Hence, a two-step purification protocol was developed which allowed obtaining 15–20 mg of rePCP4MO from 1 L culture. The rePCP4MO revealed identity with native enzyme by SDS–PAGE and N-terminal sequence analy…