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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archiv der Mathematik 45 (1985), S. 158-168 
    ISSN: 1420-8938
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archiv der Mathematik 50 (1988), S. 270-280 
    ISSN: 1420-8938
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
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  • 3
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary For a histochemical study of ubiquinones in newborn and adult mice, the hydroquinone-tetrazolium-reductase reaction was performed in cryostat serial sections of the central cerebellar nuclei. This enzyme was studied in various structures at different stages of postnatal development. The present study shows that in the central nuclei the ubiquinones display less activity during development than in the adult mouse. The histochemical maturation is slow as compared with Purkinje cells, the rest of the molecular layer, the motor nuclei of the brain stem and the anterior horns of the medulla. The relationship of these histochemical findings and the metabolic significance of changes in the patterns of ubiquinones is discussed.
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  • 4
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Although the role of the blood group antigens in the gastrointestinal tract is not well understood, alterations in blood group-related antigens have been described in some pathological processes. Thus, the knowledge of their expression under normal conditions is of special interest. Those individuals expressing their ABO blood group in exocrine epithelia and secretions are called secretors. The aim of the present study was the localization of H antigen expression in the normal human gastric epithelial cells of non-O blood group individuals. For this, a monoclonal anti-H antibody was examined by immunocytochemical methods at both the light and electron microscopic levels. In combination with enzymatic and chemical treatments, the nature of the oligosaccharide chains containing the H antigen was characterized. The selected cases were four A secretors, three A non-secretors, and three B non-secretors. The labeling of the anti-H antibody in the human stomach is described, irrespective of the blood group of the individuals. The staining was abolished when O-linked oligosaccharides were removed. Since commercially available anti-H antibodies usually also recognize other H-related antigens, the labeling of the antibody by H-related antigens cannot be dismissed. Our findings suggest the existence of H or H-related antigens in the O-linked oligosaccharides of the secretory granules of the surface, gastric pit, mucous neck, and transitional cells of the fundic mucosa, and in the intracellular canaliculi and tubulovesicular system of parietal cells. The H or H-related antigens were also localized in the apical membrane of all the cell types of the epithelial cells of the human fundic mucosa. The overall distribution of the H or H-related antigens in the stomach in non-O blood group individuals suggests the constitutive expression of an α(1,2)fucosyltransferase.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Positivity 4 (2000), S. 253-258 
    ISSN: 1572-9281
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Molecular biology reports 11 (1986), S. 137-141 
    ISSN: 1573-4978
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Modification of 40S ribosomal subunits from Saccharomyces cerevisiae with dimethylmaleic anhydride (DMMA Abbreviation: DMMA, 2,3-dimethylmaleic anhydride. ), a reagent for protein amino groups, is accompanied by loss of polypeptide-synthesizing activity and by dissociation of proteins from the particles. The protein-deficient ribosomal particles, originated from 40S subunits by treatment with dimethylmaleic anhydride at a molar ratio of reagent to particle of 250, can partially reconstitute active subunits upon addition of the corresponding released proteins, and regeneration of the modified amino groups.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 86 (1989), S. 55-63 
    ISSN: 1573-4919
    Keywords: yeast ribosomes ; ribosome disassembly ; ribosome reconstitution ; dimethylmaleic anhydride
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Yeast 60S ribosomal subunits have been dissociated by reversible modification with dimethylmaleic anhydride. Treatment with 40 μmol reagent/ml releases 35% of the protein, producing core particles inactive in polyphenylalanine synthesis, which are totally or highly deficient in 17 different proteins. This preparation of residual particles recovers 45% of the original activity upon incubation with the released proteins. The reconstituted particles can be isolated by centrifugation without loss of activity, having the protein composition of the original subunits.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 97 (1990), S. 101-111 
    ISSN: 1573-4919
    Keywords: dicarboxylic acid anhydrides ; dissociating agents ; protein-containing structures ; reversible modification of lysine residues
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Dissociation of protein-containing structures by modification of protein amino groups with dicarboxylic acid anhydrides is a mild procedure which, in some cases, offers advantages over treatment with alternative dissociating agents, such as urea, guanidine hydrochloride, detergents, high ionic strength, and extremes of pH: In addition to dissociating multimeric proteins and protein aggregates, dicarboxylic acid anhydrides are effective dissociating agents for membrane-bound proteins and nucleoprotein particles. With most dicarboxylic acid anhydrides reviewed, the introduced reagent residues can be eliminated under moderate acid conditions, which allows the purification of unmodified individual components, and the use of disassembly-reconstitution systems valuable for investigating the structural and functional roles played by the individual components of complex particles: Each reagent can be suitable for a particular purpose, depending on the required specificity of the modification and stability of the modified groups: The stability of the acylated amino groups ranges from the very stable succinylated amino groups to the very labile acylation obtained with dimethylmaleic anhydride: Between these extremes, the stability of the modified amino groups decreases stepwise in the following order: maleic, exo-cis-3,6-endoxo-Δ4-tetrahydrophthalic, citraconic, and 3,4,5,6-tetrahydrophthalic anhydride. With respect to the selectivity of the produced modification, little or no modification of hydroxyamino acid and cysteine residues has been observed with dimethylmaleic, exo-cis-3,6-endoxo-Δ4-tetrahydrophthalic, and 3,4,5,6-tetrahydrophthalic anhydrides: With the other reagents, the extent of modification of hydroxyamino acid residues increases in the order citraconic, maleic and succinic anhydride: Citraconic and maleic anhydrides can produce irreversible modification of cysteine residues, the reactivity of sulfhydryl groups being higher with maleic anhydride:
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  • 9
    ISSN: 1572-8951
    Keywords: Ozone ; photochemical modeling ; propane ; butane and Mexico
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Modification of calf thymus chromatin with the protein reagent dimethylmaleic anhydride is accompanied by dissociation of histones and non-histone proteins. Gel electrophoresis of the released proteins and of those bound to the residual chromatin showed that histone H1 is dissociated more easily than the core histones (H2A, H2B, H3 and H4). These are apparently released in the proportion in which they are present in chromatin. After regeneration of the modified amino groups by incubation at pH 6.0, the released proteins are able to bind to the residual chromatin, under two different sets of reconstitution conditions, to form nucleosome-like structures.
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