RESUMO
Air dispersion modeling over coastal regions has proven to be a remarkable challenge in the field of air quality. Many conventional plume dispersion models, such as ISC2 and HYSPLIT, are unable to model such dispersion with the precision that is necessary to accurately predict ground-level concentrations in coastal areas. Considering this, the present work was carried out with two primary objectives: i) to evaluate the effectiveness of currently available mathematical models in predicting plume dispersion over a coastal region and ii) to study the impact of sulfur dioxide emissions from a petroleum refinery over a different community located in the adjacent area. This study demonstrates that CALPUFF predictions are more reliable compared to those of the other models studied, however the operation of CALPUFF is highly data intensive and in many instances, it is difficult to obtain all required input data. This is a particular problem for regions outside ofthe United States of America where sufficient data is difficult to obtain. In addition, the study concluded that the predicted annual average SO2 concentrations in the nearby communities are well within regulatory limits.
Assuntos
Poluentes Atmosféricos/análise , Modelos Teóricos , Dióxido de Enxofre/análise , Movimentos do Ar , Previsões , Resíduos Industriais , PetróleoRESUMO
The yeast gene encoding the 95-kDa subunit of the class III gene transcription factor TFIIIC was cloned. This gene, termed TFC1 (transcription factor C, gene 1), was isolated by screening a lambda gt11 yeast cDNA expression library using a polyclonal antiserum preparation which was previously shown to specifically recognize the 95-kDa subunit of yeast TFIIIC (Parsons, M. C., and Weil, P. A. (1990) J. Biol. Chem. 265, 5095-5103). TFC1 was found to be a single copy gene which contained a continuous open reading frame about 2 kilobases in length. TFC1 was shown to encode the 95-kDa subunit of TFIIIC by several criteria. Like the authentic yeast protein, the protein encoded by TFC1 had an apparent molecular weight of 95,000. In addition, the protein encoded by the TFC1 gene bound to the same antibody species as the yeast 95-kDa subunit of TFIIIC. Last, the sizes of the cleavage products of the Escherichia coli-expressed protein were indistinguishable from those of the cleavage products of the bona fide yeast 95-kDa protein.
Assuntos
Genes Fúngicos , Fatores de Transcrição TFIII , Fatores de Transcrição/genética , Sequência de Aminoácidos , Sequência de Bases , Clonagem Molecular/métodos , DNA Fúngico/genética , DNA Fúngico/isolamento & purificação , Escherichia coli/genética , Substâncias Macromoleculares , Dados de Sequência Molecular , Peso Molecular , Oligodesoxirribonucleotídeos , Plasmídeos , RNA Mensageiro/genética , RNA Mensageiro/isolamento & purificação , Proteínas Recombinantes/isolamento & purificação , Mapeamento por Restrição , Fatores de Transcrição/isolamento & purificaçãoRESUMO
The class III gene transcription factor termed TFIIIC has been extensively purified from Saccharomyces cerevisiae. Three polypeptides of 138, 131, and 95 kDa consistently copurified with TFIIIC transcription factor activity. These polypeptides were present in approximately equimolar quantities in all TFIIIC preparations. To determine which, if any, of these polypeptides were involved in TFIIIC activity, rabbit polyclonal antibodies were generated against each of these three polypeptides purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Immunoblot analyses showed that each of the three antiserum preparations reacted uniquely with the respective polypeptide to which they had been elicited. This lack of cross-reactivity by any of the antiserum preparations suggested that these three polypeptides represented distinct unrelated gene products. Each of the three specific antiserum preparations decreased the mobility of TFIIIC-tDNA complexes in a DNA mobility shift assay. More importantly, all three antiserum preparations directly inhibited the transcription factor activity of TFIIIC. In addition, all three antiserum preparations depleted a solution of TFIIIC transcription factor activity. These results indicated that each of these three polypeptides of Mr = 138,000, 131,000, and 95,000 was a distinct and necessary component of yeast TFIIIC. Immunoblot analyses of immunoaffinity-purified TFIIIC fractions indicated that each of the three antiserum preparations alone could deplete the solution of all three polypeptides. These results suggested that these three polypeptides were tightly associated with one another in solution.
