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  • Articles  (72)
  • Physical Chemistry  (43)
  • Molecular Cell Biology  (29)
  • Wiley-Blackwell  (72)
  • 1975-1979  (72)
  • 1
    Electronic Resource
    Electronic Resource
    Preparation of nonreactive surfaces for reaction-rate studies (1976)
    New York, NY : Wiley-Blackwell
    International Journal of Chemical Kinetics 8 (1976), S. 23-24 
    Details
    ISSN: 0538-8066
    Keywords: Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/kin.550080104
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  • 2
    Electronic Resource
    Electronic Resource
    Collisional deactivation of O2(1Σg+) (1979)
    New York, NY : Wiley-Blackwell
    International Journal of Chemical Kinetics 11 (1979), S. 175-185 
    Details
    ISSN: 0538-8066
    Keywords: Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Relaxation rates for O2(1Σg+) by nonradiative pathways have been determined using the fast-flow technique. O2(1Σg+) is formed from O2(1Δg) by an energy pooling process. O2(1Δg) is generated by passing purified oxygen through a microwave discharge. Oxygen atoms are removed by distilling mercury vapor through the discharge zone. It has been observed that the wall loss rate for O2(1Σg+) decreases with increasing pressure of oxygen and thus appears to be diffusion controlled. Quenching rate constants for O2, N2, and He have been determined and found to be (1.5 ± 0.1) × 104, (1.0 ± 0.05) × 106 and (1.2 ± 0.1) × 105 l./mol·sec, respectively.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/kin.550110209
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  • 3
    Electronic Resource
    Electronic Resource
    Defective transport of thymidine by cultured cells resistant to 5-bromodeoxyuridine (1977)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 6 (1977), S. 363-374 
    Details
    ISSN: 0091-7419
    Keywords: thymidine transport ; nitrobenzylthioinosine ; bromodeoxyuridine resistances ; HeLa cells ; thymidine kinase ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A line of HeLa cells resistant to 5-bromo-2′-deoxyuridine (BUdR) was established by continuous culture in growth medium containing BUdR; during the selection period, BUdR concentrations, initially 15 μM, were gradually increased to 100 μM. Cells of a clone (HeLa/B5) established from this line were also resistant to 5-fluoro-2′-deoxyuridine (FUdR), but not to the free base, 5-fluorouracil. Although extracts of HeLa/B5 cells exhibited levels of thymidine kinase activity comparable to those of parental cells, rates of uptake of BUdR, FUdR, and thymidine into intact cells were much reduced. The kinetics of uptake of uridine and adenosine, nucleosides which appear to be transported independently of thymidine in HeLa cells, were similar for HeLa/B5 and the parental line (HeLa/0). Relative to thymidine uptake by HeLa/0 cells, that by HeLa/B5 cells was distinctly less sensitive to nitrobenzlthionosine (NBMPR), a specific inhibitor of nucleoside transport in various types of animal cells. Despite this difference in NBMPR sensitivity, both cell lines possessed the same number of high affinity NBMPR binding sites per mg cell protein. The altered kinetics of thymidine uptake and the NBMPR insensitivity of that function in HeLa/B5 cells suggest that resistance to BUdR is due to an altered thymidine transport mechanism.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400060309
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  • 4
    Electronic Resource
    Electronic Resource
    Cellular and metabolic specificity in the interaction of adhesion proteins with collagen and with cells (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 11 (1979), S. 69-78 
    Details
    ISSN: 0091-7419
    Keywords: cell adhesion ; adhesion proteins ; fibronectin ; chondronectin ; collagen substrates ; gangliosides ; cell surface ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fibronectin mediates the adhesion of fibroblasts to collagen substrates, binding first to the collagen and then to the cells. We report here that the interaction of the cells with the fibronectin-collagen complex is blocked by specific gangliosides, GD1 a and GT1, and that the sugar moieties of these gangliosides contain the inhibitory activity. The gangliosides act by binding to fibronectin, suggesting that they may be the cell surface receptor for fibronectin. Evidence is presented that other adhesion proteins or mechanisms of attachment exist for chondrocytes, epidermal cells, and transformed tumorigenic cells, since adhesion of these cells is not stimulated by fibronectin. Chondrocytes adhere via a serum factor that is more temperature-sensitive and less basic than fibronectin. Unlike that of fibroblasts chondrocyte adhesion is stimulated by low levels of gangliosides. Epidermal cells adhere preferentially to type IV (basement membrane) collagen but at a much slower rate than fibroblasts or chondrocytes. This suggests that these epidermal cells synthesize their own specific adhesion factor. Metastatic cells cultured from the T241 fibrosarcoma adhere rapidly to type IV collagen in the absence of fibronectin and do not synthesize significant amounts of collagen or fibronectin. Their growth, in contrast to that of normal fibroblasts, is unaffected by a specific inhibitor of collagen synthesis. These data indicate the importance of specific collagens and adhesion proteins in the adhesion of certain cells and suggest that a reduction in the synthesis of collagen and of fibronectin is related to some of the abnormalities observed in transformed cells.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400110108
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  • 5
    Electronic Resource
    Electronic Resource
    Energetics of galactose, proline, and glutamine transport in a cytochrome-deficient mutant of salmonella typhimurium (1977)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 6 (1977), S. 389-398 
    Details
    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
    URL: http://dx.doi.org/10.1002/jss.400060312
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  • 6
    Electronic Resource
    Electronic Resource
    Bimolecular self-reactions of phenyl-substituted phenoxyl radicals studied by flash photolysis (1979)
    New York, NY : Wiley-Blackwell
    International Journal of Chemical Kinetics 11 (1979), S. 357-374 
    Details
    ISSN: 0538-8066
    Keywords: Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Rate, equilibrium, and thermodynamic data for reaction (1) of 2,6-diphenyl-4R-phenoxyl radicals, where R==OCH3 (I), Ph (II), OC2H5 (III), O-n-C18H37 (IV), and 2,6-dicyclohexyl-4-phenylphenoxyl radical (V), in various solvents are obtained. The k1 values of radicals I to V are within (5.5 ± 1.0) × 107-(1.4 ± 0.3) × 109M-1·sec-1 in propanol. The solvent effect on k1 for radicals I and II was studied. The dimerization of radical I is diffusion-controlled in all solvent studies. The dimerization of radical II is viscosity-dependent but not diffusion-controlled. Plots of k1 against ET have a V shape. Specific solvent-solute interactions are seeming to be responsible for numerical k1 values of radicals I and II. The solvent effect is more pronounced for “slow” dimerization of radicals II than for “fast” dimerization of radicals I. The minimum k1 values correspond to pyridine and chloroform. The reaction (1) rate strongly depends upon the composition of a chloroform (S)-cosolvent binary mixture. Besides reaction (1) the following reactions proceed in binary mixture: \documentclass{article}\pagestyle{empty}\begin{document}$$ K_{14} = 0.18 \pm 0.05M^{ - 1},k_{15} = (2.0 \pm 1.0) \times 10^8 M^{ - 1} \cdot \sec ^{ - 1} $$\end{document} (radical I, S-CCL4 mixture) \documentclass{article}\pagestyle{empty}\begin{document}$$ K_{14} = 0.9 \pm 0.2M^{ - 1},k_{15} = (1.2 \pm 0.5) \times 10^7 M^{ - 1} \cdot \sec ^{ - 1} $$\end{document}(radical II, S-C6H14 mixture) \documentclass{article}\pagestyle{empty}\begin{document}$$ K_{14} = 0.45 \pm 0.10M^{ - 1},k_{15} = (9.0 \pm 2.0) \times 10^6 M^{ - 1} \cdot \sec ^{ - 1} $$\end{document}(radical II, S-CCL4 mixture)In all cases k16 ≪ k15. Factors influencing dimerization rates in strongly nonideal mixtures CH3OH-CCL4 and CH3OH-CHCl3 are discussed.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/kin.550110403
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  • 7
    Electronic Resource
    Electronic Resource
    Structure and function of cholera toxin and hormone receptors (1976)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 4 (1976), S. 99-120 
    Details
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The enterotoxin from Vibrio cholerae is a protein of 100,000 mol wt which stimulates adenylate cyclase activity ubiquitously. The binding of biologically active 125I-labeled choleragen to cell membranes is of extraordinary affinity and specificity. The binding may be restricted to membrane-bound ganglioside GMI. This ganglioside can be inserted into membranes from exogenous sources, and the increased toxin binding in such cells can be reflected by an increased sensitivity to the biological effects of the toxin. Features of the toxin-activated adenylate cyclase, including conversion of the enzyme to a GTP-sensitive state, and the increased sensitivity of activation by hormones, suggest analogies between the basic mechanism of action of choleragen and the events following binding of hormones to their receptors. The action of the toxin is probably not mediated through intermediary cytoplasmic events, suggesting that its effects are entirely due to processes involving the plasma membrane. The kinetics of activation of adenylate cyclase in erythrocytes from various species as well as in rat adipocytes suggest a direct interaction between toxin and the cyclase enzyme which is difficult to reconcile with catalytic mechanisms of adenylate cyclase activation. Direct evidence for this can be obtained from the comigration of toxin radioactivity with adenylate cyclase activity when toxin-activated membranes are dissolved in detergents and chromatographed on gel filtration columns. Agarose derivatives containing the “active” subunit of the toxin can specifically adsorb adenylate cyclase activity, and specific antibodies against the choleragen can be used for selective immunoprecipitation of adenylate cyclase activity from detergentsolubilized preparations of activated membranes. It is proposed that toxin action involves the initial formation of an inactive toxin-ganglioside complex which subsequently migrates and is somehow transformed into an active species which involves relocation within the two-dimensional structure of the membrane with direct pertubation of adenylate cyclase molecules (virtually irreversibly). These studies suggest new insights into the normal mechanisms by which hormone receptors modify membrane functions.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400040110
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  • 8
    Electronic Resource
    Electronic Resource
    Topography of outer membrane assembly in salmonella (1976)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 5 (1976), S. 103-108 
    Details
    ISSN: 0091-7419
    Keywords: outer membrane ; lipopolysaccharide ; bacteriophage ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The topography of lipopolysaccharide insertion into the outer membrane of Salmonella is discussed in context with a review of recent findings pertaining to general properties of the outer membrane, such as asymmetry and lateral mobility of surface components.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400050111
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  • 9
    Electronic Resource
    Electronic Resource
    Comparison of the structural and chemical composition of giant T-even phage heads (1976)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 5 (1976), S. 475-495 
    Details
    ISSN: 0091-7419
    Keywords: T4 giant phage ; morphogenesis ; optical/computer image processing ; protein composition ; phage capsid structure ; phage head length determination ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A study has been made of the structure of the capsids of T4D giant phage produced from mutants in gene 23 and temperature-sensitive mutants in gene 24, and T4D and T2L giant phage formed by the addition of L-canavanine followed by an L-arginine chase in the growth medium.All the giant phage capsids have been shown to be built according to the same geometrical architecture. This consists of a near-hexsagonal surface net, lattice constant 129.5 Å, folded into a left-hand T = 13 prolate icosahedron elongated along one of its fivefold symmetry axes. Their only apparent difference from wild-type T-even phage capsids is their abnormally elongated tubular part.A comparison of the capsomere morphologies and protein compositions of the giant phage capsids showed that all T4D giants are indentical but differ from T2L: The T4D capsomere has a complex (6+6+1)-type morphology, whereas the T2L has a simple 6-type. T2L phage, however, lack two capsid proteins, “soc” and “hoc”, present in T4D. The difference in capsomere morphology can therefore be related to the difference in the protein compositions of these two phage.Possible differences between the initiation and means of length regulation of giant phage heads and the aberrant polyheads are discussed.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400050406
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  • 10
    Electronic Resource
    Electronic Resource
    Pyrenesulfonyl azide as a fluorescent label for the study of protein-lipid boundaries of acetylcholine receptors in membranes (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 11 (1979), S. 327-338 
    Details
    ISSN: 0091-7419
    Keywords: AcChR-enriched membranes ; pyrenesulfonyl azide ; fluorescent probes ; photolabeling ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Acetylcholine receptor (AcChR) enriched membrane fragments from Torpedo californica electroplax were labeled by in situ photogenerated nitrenes from a hydrophobic fluorescent probe, pyrene-1-sulfonyl azide. Preferential photolabeling of membrane proteins, mainly AcChR, has been achieved and there is a pronounced exposure of the 48,000 and 55,000 molecular weight subunits of AcChR to the lipid environment of the membrane core.Covalent attachment of the photogenerated fluorescence probe does not perturb the α-neurotoxins' binding properties of membrane-bound AcChR or the desensitization kinetics induced by prolonged exposures to cholinergic agonists. Non-covalent photoproducts can be conveniently removed from labeled membrane preparations by exchange into lipid vesicles prepared from electroplax membrane lipids. Fluorescence features of model pyrene sulfonyl amide derivatives, such as fine vibrational structure of emission spectra or fluorescence lifetimes, are highly sensitive to the solvent milieu. The covalently bound probe shows similar fluorescence properties in situ. PySA photoproducts have great potential to spectroscopically monitor neurotransmitter induced events on selected AcChR subunits exposed to the hydrophobic environment of membranes.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400110308
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