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  • fluorescence decay  (3)
  • Cell & Developmental Biology  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Toward an understanding of the fluorescence intensity changes observed on fluorescein 5′-Isothiocyanate-Na+,K+-ATPase (1994)
    Springer
    Journal of fluorescence 4 (1994), S. 251-254 
    Details
    ISSN: 1573-4994
    Keywords: Fluorescence spectra ; fluorescence decay ; dissociation constants ; fluorescein 5′-isothiocyanate ; FITC-fluorescein 5′-isothiocyanate-Na+,K+-ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The fluorescence emission intensity between the Na+, and the K+ complex of Na+,K+-ATPase, labeled with fluorescein 5′-isothiocyanate (FITC), differs by 30 to 40%. Experimental studies are carried out to elucidate the physical reasons which account this intensity difference. The dissociation constant of protolysis of the covalently bound FITC and its fluorescence decay times are determined in media of different ionic compositions and are compared with the corresponding properties of a synthetic model compound. The fluorophore bound to the protein is characterized by two decay times in the nanosecond range; the model compound, by a single one. The static fluorescence intensity changes are discussed on the basis of these results.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01878459
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  • 2
    Electronic Resource
    Electronic Resource
    Conformational changes of Na,K-ATPase probed with eosin Y (1996)
    Springer
    Journal of fluorescence 6 (1996), S. 165-168 
    Details
    ISSN: 1573-4994
    Keywords: Cation binding ; fluorescence decay ; kinetics ; binding constants ; Na,K-ATPase ; eosin Y
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Time-resolved fluorescence and binding studies have been carried out on Na,K-ATPase in the presence of the fluorescent dye eosin Y to obtain thermodynamic and kinetic parameters for the interaction of the enzyme with different cations. Eosin Y binding is indicated by a 3 ns fluorescence decay process and is observed only in the presence of mono- and divalent cations. This type of cation binding is interpreted as a nonselective electrostatic interaction, with negatively charged groups of the enzyme providing a high-affinity eosin Y binding site. Eosin Y binding is observed only under conditions where the enzyme exists in the conformational state F1. The kinetic parameters of eosin Y binding have been determined employing stopped-flow fluorometry.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00732056
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Characterizing Protein Conformational Transitions of Na,K-ATPase with Antibodies by Fluorescence Spectroscopy (1998)
    Springer
    Journal of fluorescence 8 (1998), S. 115-119 
    Details
    ISSN: 1573-4994
    Keywords: FITC ; antibodies ; fluorescence decay ; Na ; K-ATPase ; pK
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Stationary and time-resolved fluorescence of FITC–Na,K-ATPase is investigated as a function of pH in the presence of different ligands, cations, and the monoclonal anti-FITC antibody 4-4-20. The binding of K+ and of the antibody leads to the same decreased fluorescence intensity level. Antibody binding is observed only under conditions where the enzyme exists in the conformational state F1, and not in the form of the Na+ or K+ complex or when it is phosphorylated with inorganic phosphate in the presence of Mg2+. For the interpretation of the results it is shown that the fluorophore is not essentially affected by an acidity change of the bound dye, so that pK variations responsible for the observed intensity changes can be excluded in favor of a static quenching process
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1022542208027
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  • 4
    Electronic Resource
    Electronic Resource
    The effect of medium pH on rate of growth, neurite formation and acetylcholinesterase activity in mouse neuroblastoma cells in cultureThis work was supported in part by grant NS11365 from the National Institute of Health, U.S. Public Health Service. A preliminary report of this investigation appeared in Fed. Proc., 34: 812, 1975. (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 91 (1977), S. 63-68 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Cell division, neurite formation and acetylcholinesterase activity were examined in a clone (NBA2) of mouse neuroblastoma cells maintained for up to 120 hours in medium with pH values between 6.6 and 8.0. Growth rate decreased as pH was reduced from 7.8 to 6.6. Generation time at pH 7.4 was 25 hours, while the rate of cell division was negligible at pH 6.6. The total number of cells at stationary phase was less at the lower pH values. Neurite formation was enhanced markedly as the pH was reduced from 7.4 to 6.6. Acetylcholinesterase activity was 5- to 8-fold greater in cells exposed to medium at pH 6.6 than in cells maintained in medium at pH 7.4. The reduction in the rate of cell division and increases in neurite formation and acetylcholinesterase activity at pH 6.6 were reversible upon exposure of the cells to pH 7.4 medium. Cell viability was greater than 90% at all medium pH values over a period of 120 hours. Uncloned T-59 mouse neuroblastoma cells were affected similarly by changes in pH. These results show that manipulation of the environmental pH can reversibly alter growth, neurite formation, and acetylcholinesterase activity of mouse neuroblastoma cells in culture.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040910107
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  • 5
    Electronic Resource
    Electronic Resource
    A mammary-derived growth inhibitor (MDGI) related 70 kDa antigen identified in nuclei of mammary epithelial cells (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 138 (1989), S. 415-423 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The aim of the present study was to investigate the expression of the mammary derived growth inhibitor (MDGI) and the subcellular localization of MDGI related antigens in bovine mammary glands. Cell-free translation of poly (A+) = RNA, immunoprecipitation with rabbit anti-MDGI-antibodies, and estimation of the relative contents of MDGI by a radioimmunoassay in mammary tissue of different functional statess revealed that the 13 kDa MDGI was dramatically increased in terminally differentiated mammary tissue compared with the proliferating tissue from pregnant animals. To address the question of tissue localizationl, polyclonal anti-MDGI antibodies and antibodies directed aganist a sythetic peptide corresponding ot residues 69 to 78 of MDGI were used. Western blotting of tissue fractions revealed the cytosolic and microsomal localization of MDGI. Additionally, both types of antibodies a 70-kDa antigeninthe unclear fractionof differentiated mammary glands. Salt extraction and DNase I digestion of isolated unclei, as well as chromatin purification, indicated an association of the 70-kDa antigen with the chromatin. By means of the immunogold technique, MDGI-related antigens were localized within euchromatic unclear regions of epithelial cells in the intact differentiated mammary gland. The immunostaining was markedly diminished in the proliferating tissue. This finding raises the possibility that MDGI and the 70-kDa antigen influence cell proliferation by acting on geneexpression within the unclei of mammary glands.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041380225
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