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  • 1
    ISSN: 1437-3262
    Keywords: Arctic Amerasian shelf Sediment carbon and nitrogen isotopes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences
    Notes: Abstract. Organic matter origins are inferred from carbon isotope ratios (δ13C) in recent continental shelf sediments and major rivers from 465 locations from the north Bering-Chukchi-East Siberian-Beaufort Sea, Arctic Amerasia. Generally, there is a cross-shelf increase in δ13C, which is due to progressive increased contribution seaward of marine-derived organic carbon to surface sediments. This conclusion is supported by the correlations between sediment δ13C, OC/N, and δ15N. The sources of total organic carbon (TOC) to the Amerasian margin sediments are primarily from marine water-column phytoplankton and terrigenous C3 plants constituted of tundra taiga and angiosperms. In contrast to more temperate regions, the source of TOC from terrigenous C4 and CAM plants to the study area is probably insignificant because these plants do not exist in the northern high latitudes. The input of carbon to the northern Alaskan shelf sediments from nearshore kelp community (Laminaria solidungula) is generally insignificant as indicated by the absence of high sediment δ13C values (–16.5 to –13.6‰) which are typical of the macrophytes. Our study suggests that the isotopic composition of sediment TOC has potential application in reconstructing temporal changes in delivery and accumulation of organic matter resulting from glacial–interglacial changes in sea level and environments. Furthermore, recycling and advection of the extensive deposits of terrestrially derived organic matter from land, or the wide Amerasian margin, could be a mechanism for elevating total CO2 and pCO2 in the Arctic Basin halocline.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 32 (1980), S. 115-115 
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 33 (1980), S. 102-102 
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 33 (1980), S. 101-101 
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 33 (1980), S. 103-103 
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Current microbiology 23 (1991), S. 33-38 
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract 125I-labeled type I collagen (Cn-I) binding of 92 fresh isolates and 18 type culture collection strains of lactobacilli was tested. More than 75% of the strains bound Cn-I. The binding was inhibited by excess of unlabeled Cn-I, gelatin, and was sensitive to proteinase K. Other proteins such as fibronectin and albumin and various carbohydrates such asD-galactose,D-fucose, andD-mannose did not inhibit the binding. Therefore, we propose binding of Cn-I to lactobacilli involving specific surface protein(s).
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract During investigation of the interaction of human lactoferrin (HLf) with variou bacteria, it was found that inStreptococcus pyogenes, HLf binding occurred to agar-rather than broth-grown cells irrespective of the nutrients used. Furthermore, binding of HLf to broth-grown, heat-killed bacteria was induced by overnight incubation on agar media or short-time exposure of the cells to water-soluble agar extract. The binding pattern was revealed in most of 92S. pyogenes strains representing various M-or T-types with no apparent type variation. The component thus bridging the attachment of HLf to the streptococcal cell surface was recovered in extracts of agar-grown cells and isolated by affinity chromatography on HLf-sepharose. By gel filtration in the presence of radiolabeled HLf, this component exhibited similar elution position as crude water-soluble agar extract. Chemical analysis identified the active HLf-binding agar component to be a galactose-rich polysaccharide (GRP). Further binding tests showed that the interaction between streptococci and GRP was stable in the presence of high molar NaCl, KSCN, or urea and was unaffected by various serum or matrix proteins or by streptococcal lipoteichoic acid; however, a moderate inhibition by heparin or bovine mucin was observed. Studies on isogenic mutants ofS. pyogenes did not support the involvement of M-protein or the hyaluronate capsule in the binding of GRP. SDS-PAGE and Western blot analyses revealed a GRP-binding protein of approximately 70 kDa in the cell-wall extracts of two strains ofS. pyogenes, types M19 and M55. Finally, the adherence of (broth-grown)3H-thymidine-labeledS. pyogenes, type M19, to the pharyngeal epithelial cell line DT-562 or to normal tonsillar epithelial cells was inhibited by GRP in a dose-related manner. We thus propose that the streptococcal GRP-binding component may represent a novel surface lectin acting as a mucosal adhesin forS. pyogenes, in accordance with previous data indicating that galactosecontaining sugar moieties may serve as ligands for the adherence of streptococci to pharyngeal cells. Our results also indicate that GRP-like components such as mucin or heparin might act to block epithelial adherence ofS. pyogenes at the mucosal level.
    Type of Medium: Electronic Resource
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