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  • 1
    Electronic Resource
    Electronic Resource
    Isolation and properties of sarcoplasmic reticulum from the fast muscles of plaice Pleuronectes platessa L. (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of fish biology 18 (1981), S. 0 
    Details
    ISSN: 1095-8649
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: This paper describes a method for the isolation of highly purified sarcoplasmic reticulum from plaice fast muscle. The interrelationships of pH, KCL, Ca2+, Mg2+, ADP and temperature have been investigated. Protein composition of plaice white muscle sarcoplasmic reticulum was found to be comparable to that described for rabbit fast muscle, with a major component of 100 000 daltons. Arrhenius plots of the Ca2+-AT Pase are linear over the range 0–30°C. Activation enthalpy (60±1.5 kJ/mol) was found to be independent of KCl concentration. The calcium concentration required to give half maximal activation of the AT Pase (KCa) was found to decrease with increasing temperature, from a maximum of 1.7 μm at 0°C to 0.55 at 20°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1095-8649.1981.tb02815.x
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  • 2
    Electronic Resource
    Electronic Resource
    Evidence for involvement of nuclear envelope nucleoside triphosphatase in nucleocytoplasmic translocation of ribonucleoprotein (1976)
    [s.l.] : Nature Publishing Group
    Nature 263 (1976), S. 165-167 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 Time course of RNA release from isolated nuclei. All experiments were carried out at 35 C in the following medium13: 50 mM Tris-HCl, pH 7.6, 25 mM KC1, 2.5 mM MgCl2, 0.3 mM MnCl2,0.5 mM CaCl2, 5.0 mM NaCl, 2.5 mM K2HPO4, 5.0 mM spermidine and 2.0 mM dithioerythrytol. O, Control; , release ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/263165a0
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  • 3
    Electronic Resource
    Electronic Resource
    Transferrin-receptor interaction and iron uptake by reticulocytes of vertebrate animals — a comparative study (1987)
    Springer
    Journal of comparative physiology 157 (1987), S. 363-371 
    Details
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Transferrin-receptor interactions and iron uptake were studied in eleven different species of vertebrate animals (3 eutherian mammals, 3 marsupials, 2 reptiles and 1 bird, amphibian and bony fish). In the initial experiments it was shown that the uptake of transferrin-bound iron by immature erythroid cells from marsupial and reptilian species occurs by receptor-mediated endocytosis as in other vertebrate animals. Reticulocytes were incubated with125I-59Fe-labelled transferrins from heterologous species and the results for iron and transferrin uptake compared with those obtained with the homologous protein. Cells from eutherian mammals were able to take up transferrin and iron from other eutherians and from the bob-tailed lizard but not from marsupials and other submammalian species. With marsupials and reptiles a similar specificity was observed, and the marsupial cells could also utilize chicken transferrin but not vice versa. The results were extended by performing competition experiments in which the cells were incubated with radiolabelled homologous transferrin in the presence of increasing concentrations of non-radioactive heterologous transferrins. From the ability of the heterologous proteins to inhibit uptake of the homologous protein relative association constants (K a 1) for the transferrin-receptor interactions could be calculated. TheseK a 1 values reflected the patterns observed in the first series of experiments. These studies demonstrate that, although specificity exists in transferrin-receptor interactions throughout the range of vertebrate animals, in several instances reactivity between widely divergent species is also observed. Hence, structural similarities have been maintained throughout evolution. Nevertheless, no evidence of interaction between transferrin and its receptor from the two divisions of the Mammalia, the eutherians and the marsupials, was observed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00693363
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  • 4
    Electronic Resource
    Electronic Resource
    Intravesicular pH and iron uptake by immature erythroid cells (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 120 (1984), S. 225-232 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The intravesicular pH of intact rabbit reticulocytes was measured by two methods; one based on the intracellular:extracellular distribution of DMO (5, 5, dimethyl + oxazolidin-2,4-dione), methylamine, and chloroquine and the other by quantitative fluorescence microscopy of cell-bound transferrin. The latter method was also applied to nucleated erythroid cells from the fetal rat liver. A pH value of approximately 5.4 was obtained with both methods and in both types of cells. Treatment of the cells with lysosomotrophic agents, metabolic inhibitors, and ionophores elevated the intravesicular pH and inhibited iron uptake from transferrin. When varying concentrations of NH4Cl were used, a close correlation was observed between the inhibition of iron uptake and elevation of the intravesicular pH. At pH 5.4 iron release from rabbit iron-bicarbonate transferrin in vitro was much more rapid than from iron-oxalate transferrin. The bicarbonate complex donates its iron to rabbit reticulocytes approximately twice as quickly as the oxalate complex. It is concluded that the acidic conditions within the vesicles provide the mechanism for iron release from the transferrin molecule after its endocytosis and that the low vesicular pH is dependent on cellular metabolism.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041200217
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  • 5
    Electronic Resource
    Electronic Resource
    Uptake of transferrin and iron by cultured rat placental cells (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 122 (1985), S. 405-409 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: This paper describes a method for the culture of rat placental cells. The method involved separation of the basal layer from the labyrinth and sequential digestion of the cells. The cells were demonstrated not to be fibroblasts and are described in terms of their appearance under the light and electron microscopes. Transferrin and iron uptake by the cells was examined and compared with results achieved using other methods of study. The results showed that transferrin bound to receptors on the cell surface and that the transferrin, once bound, was taken into the cell. Only this internalized transferrin was capable of donating iron to the cells. The iron was accumulated within the cells and did not appear to be released to the incubation medium. The apparent dissociation constant (Ka) for transferrin was found to be 6.96 × 106 M-1, a value similar to that described by earlier workers. The placental cells had 3.4 × 1011 binding sites/μg DNA, equivalent to approximately 1 × 106 sites/cell. From these data, and from the rate of accumulation of iron by the cells, the receptor turnover time was estimated as being between 5 and 10 min.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041220310
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