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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 11 (1972), S. 568-572 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 11 (1972), S. 563-568 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 73 (1951), S. 2416-2420 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 174 (1954), S. 1192-1193 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The pneumococcal product differs markedly, however, from N-acetylhyalobiuronic acid, the repeating unit of hyaluronate3 and of the oligosaccharide fractions obtained on digestion with testicular hyaluronidase2 as demonstrated in Table 1. The values indicate that the bacterial product is a ...
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 180 (1957), S. 810-811 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The presence in the leech of a potent hyaluronidase had been noted previously, including its effect on the physical properties of hyaluronic acid, the production of reducing sugars and its action as a spreading factor3. Paper chromatograms of the products of the 24-hr. digestion of sodium ...
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 168 (1951), S. 996-997 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The present communication is concerned with the isolation and characterization of a crystalline aldo-biuronic acid from sodium hyaluronate in relatively high yield, following degradation by a combination of enzymic and mild acid hydrolysis. Sodium hyaluronate (analysis3: nitrogen, 3-78; uronic ...
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  • 7
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 218 (1968), S. 774-775 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] All organisms were grown on MacConkey's agar and the polysaccharide was isolated as previously described2. The bacterial growth was washed off the plates with physiological saline and the suspension was stirred well for 2 h. The cells were then removed by centrifugation and the crude polysaccharide ...
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  • 8
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 204 (1964), S. 187-188 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] At a concentration of 0-5 per cent of the polysaccharide, a very viscous aqueous solution was obtained. Analyses showed only insignificant amounts of hexoses1, hexose-amines2, phosphate and protein. A small amount, about 5 per cent, of nucleic acid was shown to be present by measuring absorption at ...
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 147 (1991), S. 455-459 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The synthesis of metabolically labeled proteoglycans and glycosaminoglycans from medium, cell layer and substrate attached material by rat glomerular mesangial cells in culture was characterized. The cellular localization of the labeled proteoglycans and glycosaminoglycans was determined by treating the cells with Flavobacterial heparinase. Of the total sulfated glycosaminoglycans, 33% were heparan sulfate; 55% of the cell layer material was heparan sulfate; 80% of sulfated proteins in the medium were chondroitin sulfate/dermatan sulfate. Putative glycosaminoglycan free chains of heparan sulfate and chondroitin sulfate were found in both the medium and cell layer; 95% of total proteoglycans and most (90%) of the putative heparan sulfate free chains were removed from the cell layer by the heparinase, whereas only 50% of the chondroitin sulfate and 25% of dermatan sulfate were removed. Large amounts of hyaluronic acid labeled with 3H glucosamine were found in the cell layer. In summary, approximately 60% of total sulfated glycoproteins was in the form of putative glycosaminoglycan free chains. Thus rat mesangial cells may synthesize large amounts of putative glycosaminoglycan free chains, which may have biological functions in the glomerulus independent of proteoglycans.
    Additional Material: 1 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 135 (1988), S. 189-199 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The synthesis and turnover of metabolically labeled proteoglycans from medium, cell layer, and substratum-associated compartments were characterized in four cell lines of fibroblastic origin, including a fibrosarcoma line, and in the murine melanoma cell type, B16.F10. Substantial differences were apparent between the various cell types with regard to quantities, hydrodynamic sizes, and compartmentalization of labeled product. Such variations were greater between the different cell lines than between separately labeled cultures of the same cell type. Greater than 85% of cell-associated proteoglycans were accessible to glycosaminoglycan-degrading enzymes added to the medium of monolayer cultures, demonstrating their principal location to be external to the cell membrane. Apparent glycosaminoglycan free chains, determined by a lack of change in hydrodynamic size following alkaline elimination, were among the products from each cell line and were similarly found to be in a principally pericellular location. Results from label-chase studies demonstrated apparent independent kinetics for proteoglycans and glycosaminoglycan free chains, with little conclusive evidence for precursor-product relationships. Also, their processing by the cells was different, since the proteoglycans were shed largely unchanged into the medium for the three cell lines evaluated, whereas the free chains were not recoverable from the medium in significant amounts. The latter observation suggests the internalization of cell surface-associated free chains and their depolymerization at an intracellular site. The results, which indicate that the content, cellular disposition, and turnover of proteoglycans are quite variable between the cell lines studied, may reflect fundamental cell type-specific specialization in the metabolism of these complex substances. Furthermore, the data raise the interesting possibility that glycosaminoglycan free chains may have biological functions at the cellular level, independent of proteoglycans.
    Additional Material: 8 Ill.
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