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An economics advisor on test strategy planning for complex electronic boardsEbhogiaye, Ijeoma N. January 1998 (has links)
No description available.
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Analytical methods for the congener specific determination of polychlorinated biphenols in environmental and food samplesChewe, Derrick January 1997 (has links)
No description available.
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An investigation into the extraction and analysis of polychlorinated biphenyls from various foodstuffsMills, Andrew G. January 1994 (has links)
No description available.
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The fate and behaviour of polychlorinated dibenzo-p-dioxins, dibenzofurans and polychlorinated biphenyls in sewage sludge : amended agricultural soils and their potential transfer into terrestrial foodchain via lactating cattleSewart, Andrew Paul January 1994 (has links)
No description available.
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Polychlorinated biphenyls and other organic contaminants in the Welsh populationDuarte-Davidson, Raquel V. January 1992 (has links)
No description available.
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Biochemical studies on the toxicity and carcinogenicity of PCBs and related compoundsBazara, Salem Mohammed January 1988 (has links)
No description available.
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Bioavailability of chlorinated biphenyls and their selected metabolites in soilsWalters, Mary Jane January 1998 (has links)
No description available.
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Trace analysis and chemistry of polychlorinated biphenylsFernandes, A. R. January 1988 (has links)
No description available.
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The enzymatic oxidation of polychlorinated organicsJones, Jonathan Peter January 2000 (has links)
No description available.
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Cloning, expression and characterisation of a single-chain antibody fragment to the herbicide paraquatGraham, Barbara Monica January 1995 (has links)
New economically viable methods for the detection and removal of organic pollutants from water samples are needed to meet modern safety requirements. Development of techniques to produce antibody fragments in Escherichia coli (E. coli) have provided the opportunity to exploit antibodies as specialised chemicals for affinity detection and removal technologies. The variable heavy and light antibody domains of the anti-paraquat monoclonal antibody PQXB1/2 have been cloned into the single-chain antibody (scAb) expression vector, pBG1. Anti-paraquat scAb (0.1-0.4 mg/L bacterial culture) was expressed in E. coli. Characterisation of scAb by antigen binding profile and competition ELISA showed it to have a sensitivity one order of magnitude below that of the parent monoclonal. ScAb was purified as a monomer or dimer and analysed by HPLC size exclusion chromatography. When immobilised on polystyrene beads the scAb could remove 85% of paraquat-bovine serum albumin conjugate from solution in a single step.
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