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  • Life Sciences  (3)
  • MASERS
  • Wiley-Blackwell  (3)
  • 1970-1974  (3)
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Verlag/Herausgeber
  • Wiley-Blackwell  (3)
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  • 1
    Digitale Medien
    Digitale Medien
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 1 (1973), S. 382-384 
    ISSN: 0091-7419
    Schlagwort(e): Life Sciences ; Molecular Cell Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Cyclic AMP appears to regulate cell growth. Cyclic AMP levels are high in normal chicken embryo fibroblasts and drop to very low levels when the cells are transformed by the Bryan high-titer strain of Rous sarcoma virus. Cells infected with a temperature-sensitive mutant of the virus have normal levels of cyclic AMP at the nonpermissive (nontransforming temperature), but when the cells are shifted to the permissive (transforming) temperature the cyclic AMP levels rapidly fall to values that are found in transformed cells. Studies on the adenylate cyclase and cyclic AMP phosphodiesterase in normal and transformed chicken embryo fibroblasts have shown that the adenylate cyclase is greatly decreased in the transformed cells whereas the phosphodiesterase is increased. The decrease in adenylate cylcase activity is the result of an increase in the Km of the substrate and a loss of a magnesium ion activator site. The increase in phosphodiesterase activity is the result of an increase in total phosphodiesterase activity and a decrease in the negative cooperativity of plasma membrane bound phosphodiesterase. Thus the fall in cyclic AMP levels that occurs on transformation can be correlated with changes in the activity of adenylate cyclase and cyclic AMP phosphodiesterase.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 2 (1974), S. 558-581 
    ISSN: 0091-7419
    Schlagwort(e): Life Sciences ; Molecular Cell Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Internal dialysis techniques have been used to examine the influence of external and internal cations on Ca efflux from ATP-depleted squid axons. The main observation is that Ca efflux is promoted by external Na and inhibited by internal Na. The Na0 -dependent Ca efflux appears to be a function of [Na]03, and is also affected by the membrane potential; a 25 mV depolarization may cause as much as an e-fold decrease in Ca efflux. These data are consistent with a counter-transport exchange of 3Na+-for-1Ca2+. A Ca0-dependent Ca efflux has also been observed; it is prominent in Na sea water or Le sea water, and is markedly diminished in choline sea water. This flux is consistent with the idea of a Ca-Ca exchange diffusion process. Taken together, the Na0 - and the Ca0 -dependent Ca effluxes fit a two-site model for carrier-mediated Ca transport; one site binds two Na+ or one Ca2+, while the second site can bind either one Na+ or one Li+. The data reported here suggest that both sites must be filled on the inward journey, but that only the Ca-binding site need be occupied on the outward journey of the carrier. A mechanism of this type could derive sufficient energy from the Na and voltage gradients to maintain a [Ca2+]0/[Ca2+]i concentration ratio of about 104 in the absence of ATP. The present experiments do not, however, rule out the possible participation of a metabolically driven Ca transport mechanism in vivo.
    Zusätzliches Material: 14 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 2 (1974), S. 138-149 
    ISSN: 0091-7419
    Schlagwort(e): Life Sciences ; Molecular Cell Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: The formation of fibrin gels involves many operations which are fundamental to other assembly schemes, including limited proteolysis, spontaneous associations, and covalent stabilization. Despite a quarter century of intensive effort by a large number of laboratories, the orientation of the fundamental units in the gel is not known, nor, for that matter, is the arrangement of the subunit chains within the parent fibrinogen molecule. In this article some symmetry considerations are discussed in light of the geometry of the starting molecules and conditions necessitated by the covalent stitching which occurs after gel formation. Only a dimeric molecule in which the twofold symmetry axis coincides with a minor axis of an elongated fibrinogen molecule satisfies all the conditions.
    Zusätzliches Material: 11 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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