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  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 144 (1939), S. 751-752 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] ATTEMPTS to obtain cell-freo enzyme preparations of animal origin effecting deamination of the monocarboxylic l-amino acids have hitherto been practically unsuccessful. (Specific enzymes deaminizing d-amino-acids and l-amino dicarboxylia acids have been obtained in solution and purified by ...
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of experimental biology and medicine 78 (1974), S. 1369-1371 
    ISSN: 1573-8221
    Keywords: sulfoglycosaminoglycans ; polysaccharides ; heparin ; protein-chondroitin-4-sulfate ; hexamminecobalt (III)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The hexamminecobalt (III) cation forms complexes with protein-chondroitin-4-sulfate and heparin in dilute solutions, interacting with these biopolymers with all three of its valencies. The conditions disturbing the results of determinations of the total content of anionic groups in sulfoglycosaminoglycans on the basis of the quantity of hexamminecobalt (III) bound with them were established.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of experimental biology and medicine 83 (1977), S. 320-324 
    ISSN: 1573-8221
    Keywords: hyaluronate ; protein-chondroitin-4-sulfate ; heparin ; red blood cells ; aggregation ; adhesion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The action of potassium hyaluronate (HUA) and protein-chondroitin-4-sulfate (PCS) on aggregation and adhesion of rabbit red cells suspended in physiological saline was studied. The ability of HUA and PCS to produce nonspecific and reversible aggregation of red cells was shown to be attributable to the property of these biopolymers of creating complex structures of the osmotic mesh and molecular sieve type in solutions, which displace the cells from the space they occupy and concentrate them in the smallest possible volume. Various fractions of heparin, which do not create such structures in solutions, do not cause the formation of separate, clearly demarcated aggregates of red cells but prevent the aggregating action of HUA and PCS when the concentrations of these biopolymers are insufficient for complete red cell aggregation. It is suggested that the aggregating action of HUA and PCS, which is essential for adhesion to take place, is one of the universal biological functions and is manifested not only toward red cells, but also toward other cells and various tissue elements.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of experimental biology and medicine 82 (1976), S. 1510-1512 
    ISSN: 1573-8221
    Keywords: hyaluronate ; protein ; chondroitin-4-sulfate ; gelatin ; structural-mechanical strength and swelling of gels
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Structural-mechanical strength and swelling of gels consisting of gelatin and potassium hyaluronate (PHY) or potassium protine-chondroitin-4-sulfate (PPCS) were shown to depend on the ratio between the components. With low concentrations of PHY and PPCS the minimum of structural-mechanical strength coincided with the maximum of swelling of the gels. In zones of neutralization of the positive electric charges of gelatin by macropolyanions, high structural-mechanical strength of the gels coincided with the minimum of swelling. In high concentrations of PHY, structural-mechanical strength and swelling of the gel became equal to the values characteristic of a gel consisting of gelatin only, but in high concentration of PPCS there was an additional parallel increase in this strength and in swelling of the gel.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of experimental biology and medicine 75 (1973), S. 643-645 
    ISSN: 1573-8221
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of experimental biology and medicine 82 (1976), S. 1785-1788 
    ISSN: 1573-8221
    Keywords: structural glycoprotein of connective tissue ; complexes with protein-chondroitin-4-sulfate and heparin ; hyaluronic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Structural glycoprotein (SGP) of connective tissue isolated from bovine heart valves and nasal septal cartilage forms water-soluble complexes with protein-chondroitin-4-sulfate and with various fractions of heparin. SGP does not form these complexes with hyaluronic acid. It is postulated that this phenomenon plays an important role in the formation of collagen and elastic fibers.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of experimental biology and medicine 87 (1979), S. 108-111 
    ISSN: 1573-8221
    Keywords: proteoglycans ; protein-chondroitin-keratan sulfate ; hyaluronic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Chemically isolated individual preparations of the unaggregated fraction of protein-chondroitinkeratan sulfate (PCKS) from hyaline cartilage and of hyaluronic acid (HUA) from the vitreous body of the eye and umbilical cord were investigated electron-microscopically. PCKS and HUA in films without cytochrome c consisted of granules and differed in their structural organization. In films with cytochrome c, proteoglycans appeared as a network of thin fibrils and they differed more clearly in their macromolecular organization. Complexes formed in mixtures of the two proteoglycans as a result of noncovalent interaction. Uranyl acetate stains proteoglycans well, especially PCKS without cytochrome c.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of experimental biology and medicine 98 (1984), S. 1330-1334 
    ISSN: 1573-8221
    Keywords: proteoglycans ; aggregation ; adhesion ; erythrocytes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of experimental biology and medicine 72 (1971), S. 1269-1271 
    ISSN: 1573-8221
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of experimental biology and medicine 79 (1975), S. 158-159 
    ISSN: 1573-8221
    Keywords: blood coagulation ; heparin and its fractions ; anticoagulant ability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The anticoagulant ability of a heparin fraction containing four sulfuric acid residues per disaccharide structural unit of the macromolecule is 1.40 times greater than that of a fraction containing three sulfuric acid residues per unit.
    Type of Medium: Electronic Resource
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