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  • 1995-1999
  • 1975-1979  (105)
  • 1920-1924
  • 1977  (105)
  • Life Sciences  (105)
  • 101
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 7 (1977), S. 307-322 
    ISSN: 0091-7419
    Keywords: myoblast differentiation ; Con-A ; extracellular filamentous matrix ; insulin ; dexamethasone ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Myoblasts are mononucleated cells and associated with differentation undergo cell fusion and become multinucleated. The current studies have examined cell surface dynamic changes of Concanavalin A lectin receptor mobility and the role of hormones in modulating myoblast differentiation. A uniform distribution of Con-A receptors is observed in undifferentiated cells when reacted with Con-A at 37°C. Cells from differentiating cultures or fully differentiated myotubes reacted similarly at 37°C show a significant redistribution of Con-A into patches, “caps,” and endocytic vesicles containing Con-A. If undifferentiated and differentiated cells are first prefixed with glutaraldehyde then reacted with Con-A continuous distribution of Con-A is seen across the cell surface. This suggests redistribution of Con-A and its receptors occurs in differentiated cells reacted with lectin at 37°C. It is further shown that insulin (10 μg/ml) significantly enhances myoblast differentiation but that this occurs after an apparent stimulation of proliferation. In contrast to insulin, dexamethasone (10 μM and 100 μM) profoundly inhibits myoblast differentiation while having different effects on proliferation; 10 μM dex stimulates cell growth while 100 μM dex suppresses cell proliferation. Lastly, an extracellular filamentous matirix which binds Con-A is observed at the ultrastructural level in high density cultures. No significant redistribution of Con-A is observed on this matrix in distinction to the redistribution observed on the cell membrane in differentiated cells.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
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  • 102
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 6 (1977), S. 345-353 
    ISSN: 0091-7419
    Keywords: Ca2+ + Mg2+ ATPase ; transport ; inophore ; energy coupling ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The 20K dalton fragment of Ca2+ + Mg2+-ATPase obtained from the tryptically digested sarcoplasmic reticulum has been further purified using Bio-Gel P-100. This removed low-molecular-weight UV-absorbing and positive Lowry-reacting contaminants. The ionophoric activity of the 20K fragment in both oxidized cholesterol and phosphatidylcholine: cholesterol membranes is unaltered by this further purification. The 20K selectivity sequence in phosphatidylcholine: cholesterol membranes is Ba2+ 〉 Ca2+ 〉 Sr2+ 〉 Mn2+ Mg2+.Digestion of intact sarcoplasmic reticulum vesicles with trypsin, which results in the dissection of the hydrolytic site (30K) from the ionophoric site (20K), is shown to disrupt energy transduction between ATP hydrolysis and calcium transport. This further implicates the 20K dalton fragment as a calcium transport site.These data and previous evidence are discussed in terms of a proposed model for the ATPase molecular structure and the mechanism of cation transport in sarcoplasmic reticulum.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 103
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 6 (1977), S. 333-344 
    ISSN: 0091-7419
    Keywords: calcium transport ; quinacrine fluorescence ; rubidium transport ; sucrose transport ; lipopolysaccharide antibody ; scanning electron microscopy ; topology ; membrane vesicles ; Azotobacter vinelandii ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Membrane vesicles were prepared from Azotobacter vinelandii spheroplasts by lysis in either potassium phosphate (pH 7.0) or Tris1-acetate (pH 7.8) buffers. These 2 types of preparations differ considerably in their properties: (1) Examination by scanning electron microscopy reveals that the Pi vesicles consist primarily of closed structures 0.6-0.8 μm in diameter with a rough or particulate surface similar to that of spheroplasts. The Tris vesicles are significantly smaller, 0.1-0.3 μm in diameter, and have a much smoother surface structure. (2) Antisera from rabbits immunized with A. vinelandii lipopolysaccharide antigen will agglutinate Pi vesicles but not Tris vesicles. (3) Tris vesicles have a fourfold higher specific activity of latent H+-ATPase than Pi vesicles. After exposure to Triton X-100 similar ATPase activities are observed for both types of vesicles. (4) Pi vesicles transport calcium in the presence of ATP or lactate at less than 30% of the rates observed for Tris vesicles. (5) Tris vesicles have less than 22% of the transport capacity of Pi vesicles for accumulation of labeled sucrose and less than 3% of the capacity for valinomycin-induced uptake of rubidium observed during respiration. (6) Quinacrine fluorescence intensity is reduced by 30% during lactate oxidation and 20% during ATP hydrolysis by Tris vesicles. Under similar conditions, fluorescence in Pi vesicles is quenched by only 7% and less than 2%, respectively. These findings suggest that Pi vesicles have the normal orientation of the intact cell whereas Tris vesicles have an inverted topology.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 104
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 6 (1977), S. 389-398 
    ISSN: 0091-7419
    Keywords: amino acid transport ; transport energetics ; cytochrome-deficient mutant ; shock-sensitive transport ; shock-resistant transport ; Salmonella typhimurium ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The effect of inhibitors and uncouplers on the osmotic shock-sensitive transport systems for glutamine and galactose (by the β-methyl galactoside permease) was compared to their effect on the osmotic shock-resistant proline and galactose permease systems in cytochrome-deficient cells of Salmonella typhimurium SASY28. Both osmotic shock-sensitive and -resistant systems were sensitive to uncouplers and to inhibitors of the membrane-bound Ca2+, Mg2+-activated adenosine triphosphatase. This suggests that uptake by both types of systems is energized in these cells by an electrochemical gradient of protons formed by ATP hydrolysis through the ATPase.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 105
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 6 (1977), S. 383-388 
    ISSN: 0091-7419
    Keywords: protonmotive force ; sodium ions ; Streptococcus lactis ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Energized cells of Streptococcus lactis conserve and transduce energy at the plasma membrane in the form of an electrochemical gradient of hydrogen ions (Δp). An increase in energy-consuming processes, such as cation transport, would be expected to result in a change in the steady state Δp. We determined the electrical gradient (ΔΨ) from the fluorescence of a membrane potential-sensitive cyanine dye, and the chemical H+ gradient (ΔpH) from the distribution of a weak acid. In glycolyzing cells incubated at pH 5 the addition of NaCl to 200 mM partially dissipated the Δp by decreasing ΔΨ, while the ΔpH was constant. The Δp was also determined independently from the accumulation levels of thiomethyl-β-galactoside. The Δp values decreased in cell fermenting glucose at pH 5 or pH 7 when NaCl was added, while the ΔpH values were unaffected; cells fermenting arginine at pH 7 showed similar effects. Thus, these nongrowing cells cannot fully compensate for the energy demand of cation transport.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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