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Content available remote PAH soil concentrations in the vicinity of charcoal kilns in Bieszczady
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EN
The aim of the study was to assess the degree of soil contamination by PAHs in the area of charcoal kiln basis, located in the East Carpathian Biosphere Reserve. The concentrations of PAH in soil samples derived from various sampling locations pointed to a strong or a very strong contamination of the ecosystem by these compounds (8,95 μg×g^-1 –283,53 μg×g-1). PAH concentrations in the soil differed significantly between the sampling locations. Analysis of samples from different soil layers (to 30 cm) pointed to a threat of washing out into groundwater. The highest concentrations of PAH corresponded to soil samples collected near kilns (distance of 1.5 m), and were in the range of 17.81 μg×g^-1 – 435.54 μg×g^-1. PAH content in soil gradually decreased with increasing distance from the kilns to values < 1 μg×g^-1. The analysis of the data from three sampling periods (June-August) pointed to higher concentrations of PAHs in soil collected in the middle of the burning season, what was probably due to their more intense emission and a relatively small amount of precipitation.
PL
W niniejszej pracy zostały przedstawione dane dotyczące zanieczyszczenia gleb przez wielopierścieniowe węglowodory aromatyczne (WWA) w okolicy wypalarni węgla drzewnego, usytuowanych na terenie Rezerwatu Biosfery Karpaty Wschodnie. Celem badań była ocena stopnia zanieczyszczenia gleb przez WWA oraz zasięgu emisji zanieczyszczeń z poszczególnych wypalarni. Stężenia WWA w glebach pochodzących z poszczególnych stanowisk badawczych wskazywały na silne lub bardzo silne zanieczyszczenie ekosystemu tymi związkami (8,95 μg×g^-1 – 283,53 μg×g^-1). Stężenia WWA w glebie różniły się istotnie pomiędzy badanymi stanowiskami. Analiza próbek pochodzących z warstw gruntowych (do 30 cm) wskazywała na zagrożenie przedostawania się części z tych zanieczyszczeń do wód gruntowych. Najwyższe stężenia WWA pochodziły z próbek gleby pobranych najbliżej wypalarni (1,5 m) i mieściły się w przedziale 17,81 μg×g^-1 – 435,54 μg×g^-1. Zawartość WWA w glebie malała stopniowo wraz z odległością od retort (do 60 m), osiągając jednak nadal wysokie wartości dla dwóch najintensywniej działających wypalani (4 i 6): 0,44 μg×g^-1 – 69,3 μg×g^-1. Analiza danych z trzech poborów (czerwiec - październik) wskazuje na wyższe stężenia WWA w glebie w środku sezonu wypałowego, co wynika prawdopodobnie z najintensywniejszej ich emisji oraz stosunkowo małej ilości opadów atmosferycznych.
EN
Tn and sialyl-Tn carbohydrate structures, first identified in glycophorins of persons with the rare Tn syndrome, were found to be present on the surface of most cancer cells. In this article, the studies on Tn and sialyl-Tn antigens as diagnostic and prognostic tumor markers and as immunogens in vaccines for cancer immunotherapy are shortly reviewed.
EN
Carcinoembryonic antigen (CEA) is an oncofoetal cell surface glycoprotein that serves as an important tumour marker for colorectal and some other carcinomas. Its immunoglobulin-like structure places CEA within the immunoglobulin superfamily. CEA functions in several biological roles including homotypic and heterotypic (with other CEA family members) cell adhesion. Cell-cell interaction can be modulated by different factors, e.g., post-translational modifications such as glycosylation. The pur­pose of this study was to examine whether changes in carbohydrate composition of CEA oligosaccharides can influence homotypic (CEA-CEA) interactions. In order to modulate glycosylation of CEA we used two different glycosylation mutants of Chi­nese hamster ovary (CHO) cells, Lec2 and Lec8. Lec2 cells should produce CEA with nonsialylated N-glycans, while Lec8 cells should yield more truncated sugar struc­tures than Lec2. Parental CHO (Pro5) cells and the glycosylation deficient mutants were stably transfected with CEA cDNA. All three CEA glycoforms, tested in a solid-phase cell adhesion assay, showed an ability to mediate CEA-dependent cell ad­hesion, and no qualitative differences in the adhesion between the glycoforms were observed. Thus, it may be assumed that carbohydrates do not play a role in homotypic adhesion, and the interactions between CEA molecules depend solely on the poly- peptide structure.
EN
A higher content of Tn and sialyl-Tn receptors in glycophorin A of blood group N than in that of blood group M was suggested by reactions with anti-Tn lectins. Analysis of [^-elimination products of two blood group M and two blood group N preparations by gas liquid chromatography-mass spectrometry showed that GalNAc- -ol was detectable in minor amounts in all analyzed samples and its content was higher in the products obtained from desialylated antigens. Moreover, the content of Gal N Ac- -ol detected in blood group N samples was almost twice as high as in respective blood group M samples. Since blood group M and N antigens differ in two amino-acid residues, our results support the existence of sequence-dependent differences in efficiency of substitution of glycophorin GalNAc-Ser/Thr residues with galactose.
EN
 Duffy antigen is a glycosylated blood group protein acting as a malarial and chemokine receptor. Using glycosylation mutants we have previously demonstrated, that all three potential glycosylation sites of the Duffy antigen are occupied by N-linked oligosaccharide chains. In this study, wild-type Duffy glycoprotein and three mutants, each containing a single N-glycan, were used to characterize the oligosaccharide chains by lectin blotting and endoglycosidase digestion. The positive reaction of all the recombinant Duffy forms with Datura stramonium and Sambucus nigra lectins showed that each Duffy N-linked glycan contains Galβ1-4GlcNAc units terminated by (α2-6)-linked sialic acid residues, typical of complex oligosaccharides. The reactivity with Aleuria aurantia and Lens culinaris lectins suggested the presence of (α1-6)-linked fucose at the N-glycan chitobiose core. The failure of the Galanthus nivalis and Canavalia ensiformis lectins to bind to any of the Duffy mutants or to the wild-type antigen indicated that none of the three Duffy N-glycosylation sites carries detectable levels of high-mannose oligosaccharide chains. Digestion of Duffy samples with peptide N-glycosidase F and endoglycosidase H confirmed the presence of N-linked complex oligosaccharides. Our results indicate that Duffy antigen N-glycans are mostly core-fucosylated complex type oligosaccharides rich in N-acetyllactosamine and terminated by (α2-6)-linked sialic acid residues.
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