Removal of naphthalene and phenanthrene using aerobic membrane bioreactor

The removal of polycyclic aromatic hydrocarbons by membrane bioreactor (MBR) under aerobic conditions had been studied using naphthalene (NAP) and phenanthrene (PHE) as model compounds. Three MBRs with submerged ultra-filtration hollow fiber membranes were operated applying different operational conditions during 6.5 months. Complete NAP and PHE removal was obtained applying loads of 7 gNAP kgTSS^?1 day^?1 and 0.5 gPHE kgTSS^?1 day^?1, while the organic loading rate was adjusted to 0.26 kgCOD kgTSS^?1 day^?1, with the biomass concentration being 6000 mgTSS L^?1, the hydraulic retention time (HRT) 8 h and the solids retention time (SRT) 30 days. Load increases, as well as HRT and SRT reductions, affected the NAP and PHE removals. Biodegradation was found to be the major NAP and PHE removal mechanism. There was no NAP accumulation in the biomass. Low PHE quantities remain sorbed in the biomass and the contribution of the sorption in the removal of this compound was estimated to be less than 0.01 %. The volatilization does not contribute to the PHE removal in MBRs, but the contribution of NAP volatilization can reach up to 0.6 % when HRT of 8 h is applied.     

The lymphocyte restimulation system: Evaluation by intra-HLA-D group priming

Homozygous typing cells (HTC) were primed, using responding and stimulating lymphocytes of the same HLA-D groups. These intra-HLA-D group primings showed strong specific responses. Restimulation by HLA-D heterozygous and homozygous cell panels showed no correlation between the restimulating determinant and HLA-D. On the other hand, an unrelated individual, not carrying Dw4 and primed to Dw4 HTC, is restimulated by three of four Dw4-HTC. Thus, one non-HLA-D-associated restimulating determinant and another HLA-D-associated determinant could be identified. The differences among the four Dw4 HTC recognized in secondary MLC could reflect either recognition of separate gene products or recognition of separate determinants on the same gene product.     

Nitrogen Oxyanion-dependent Dissociation of a Two-component Complex That Regulates Bacterial Nitrate Assimilation

Nitrogen is an essential nutrient for growth and is readily available to microbes in many environments in the form of ammonium and nitrate. Both ions are of environmental significance due to sustained use of inorganic fertilizers on agricultural soils. Diverse species of bacteria that have an assimilatory nitrate/nitrite reductase system (NAS) can use nitrate or nitrite as the sole nitrogen source for growth when ammonium is limited. In Paracoccus denitrificans, the pathway-specific two-component regulator for NAS expression is encoded by the nasT and nasS genes. Here, we show that the putative RNA-binding protein NasT is a positive regulator essential for expression of the nas gene cluster (i.e. nasABGHC). By contrast, a nitrogen oxyanion-binding sensor (NasS) is required for nitrate/nitrite-responsive control of nas gene expression. The NasS and NasT proteins co-purify as a stable heterotetrameric regulatory complex, NasS-NasT. This protein-protein interaction is sensitive to nitrate and nitrite, which cause dissociation of the NasS-NasT complex into monomeric NasS and an oligomeric form of NasT. NasT has been shown to bind the leader RNA for nasA. Thus, upon liberation from the complex, the positive regulator NasT is free to up-regulate nas gene expression.     

Phosphatidylinositol linkage of a truncated form of the platelet-derived growth factor receptor

The platelet-derived growth factor (PDGF) receptor is usually anchored to the plasma membrane through a membrane-spanning hydrophobic amino acid sequence that splits the molecule into two approximately equal pieces, an amino-terminal external domain that contains the binding site for PDGF and a carboxyl-terminal cytoplasmic domain that includes the tyrosine kinase coding sequences. Here we report the expression of a truncated PDGF receptor that consists of the extracellular domain without the transmembrane and cytoplasmic domains. Unexpectedly, this form of the receptor that lacks a hydrophobic membrane-anchoring sequence was bound to the membrane and was not secreted into the culture media. Conventional methods to dissociate noncovalent protein-protein interactions failed to release the protein from the membrane. When the transmembrane and cytoplasmic sequences were artificially deleted from the PDGF receptor, the truncated extracellular domain was anchored to the membrane through phospholipids and could be released by phospholipase C treatment. This truncated form of the receptor bound PDGF with an affinity 5-20-fold lower than the full-length receptor.     

Long term regulation of nucleoside transport by thyroid hormone (T3) in cultured chromaffin cells

The adenosine transport in cultured chromaffin cells was increased by the presence of triiodo-l-thyronine (T₃) throughout the prolonged period studied. The V_max values of this transport obtained in absence and presence of 1 M T₃ were 36.21±2.1 and 44.17±3.5 (means±SD) pmol/10⁶cells/min respectively for 26 hours incubation-time with the hormone. The K_m values were not significantly modified. The number of adenosine transporters in cultured chromaffin cells, measured by [³H]nitrobenzylthioinosine (NBTI) binding, was increased by 1 M T₃ for 26 hours incubation-time. The values of binding sites per cell were 33,500±3,000 and 40,153±3,700 in absence and presence of T₃ respectively, without changing the K_d constant. When the transport studies were carried out in presence of cycloheximide, an inhibitor of protein synthesis, the adenosine transport capacity decreased with a half-life values of 23.9±2.8 and 24.3±2.1 hours both in the presence or absence of T₃ respectively. When cells were incubated in the presence of both T₃ and cycloheximide, not only the activatory effect of T₃ was completely abolished but also adenosine transport was decreased to the same extent as with cycloheximide alone. These results indicated that T₃ activation of adenosine transport in chromaffin cells required the protein-synthesizing mechanism.     

Production of colonization factor antigen II of enterotoxigenicEscherichia coli is subject to catabolite repression

Experiments were performed to study the effect of glucose on the production of the fimbrial colonization factor CFA/II of enterotoxigenicEscherichia coli (ETEC). The production of the CFA/II antigen was examined by electron microscopy, quantitative ELISA, and hemagglutination. The results showed that addition of 1% glucose to the growth medium drastically decreased CFA/II production, whereas addition of glycerol or sodium acetate did not have any effect. Bacteria grown in the presence of 1% glucose were essentially devoid of CFA/II fimbriae when examined under the electron microscope. Addition of 1 mM cAMP reversed the repressive effect of glucose, suggesting that the glucose suppression on CFA/II synthesis is via the mechanism of catabolite repression.     

Pigment patterns in mutants affecting the biosynthesis of pteridines and xanthommatin in Drosophila melanogaster

Eye-color mutants of Drosophila melanogaster have been analyzed for their pigment content and related metabolites. Xanthommatin and dihydroxanthommatin (pigments causing brown eye color) were measured after selective extraction in acidified butanol. Pteridines (pigments causing red eye color) were quantitated after separation of 28 spots by thin-layer chromatography, most of which are pteridines and a few of which are fluorescent metabolites from the xanthommatin pathway. Pigment patterns have been studied in 45 loci. The pteridine pathway ramifies into two double branches giving rise to isoxanthopterin, drosopterins, and biopterin as final products. The regulatory relationship among the branches and the metabolic blockage of the mutants are discussed. The Hn locus is proposed to regulate pteridine synthesis in a step between pyruvoyltetrahydropterin and dihydropterin. The results also indicate that the synthesis and accumulation of xanthommatin in the eyes might be related to the synthesis of pteridines.Support for this work was provided to J.F. in part by a grant from the Ministerio de Universidades e Investigación (Spain) and to F.J.S. by a grant from the Ministerio de Educación y Ciencia (Spain).