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  • 1
    Electronic Resource
    Electronic Resource
    Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergents (1973)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 1 (1973), S. 233-248 
    Details
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Treatment of isolated human erythrocyte membranes with Triton X-100 at ionic strength ⋍0.04 preferentially released all the glycerolipid and glycoprotein species. At low ionic strength, certain nonglycosylated polypeptides were also selectively solubilized. The liberated polypeptides were free of lipids, but some behaved as if associated into specific oligomeric complexes. Each detergent-insoluble ghost residue appeared by electron microscopy to be a filamentous reticulum with adherent lipoid sheets and vesicles. The residues contained most of the membrane sphingolipids and the nonglycosylated proteins. The polypeptide elution profile obtained with nonionic detergents is therefore nearly reciprocal to that previously seen with a variety of agents which perturb proteins. These data afford further evidence that the externally-oriented glycoproteins penetrate the membrane core where they are anchored hydrophobically, whereas the nonglycosylated polypeptides are, in general, bound by polar associations at the inner membrane surface. The filamentous meshwork of inner surface polypeptides may constitute a discrete, self-associated continuum which provides rather than derives structural support from the membrance.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400010308
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  • 2
    Electronic Resource
    Electronic Resource
    Heterogeneity in the conformation of different protein fractions from the human erythrocyte membrane (1976)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 4 (1976), S. 161-168 
    Details
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have isolated 5 families of proteins from human red blood cell membranes and characterized their secondary structure by ultraviolet circular dichroism measurements. The protein families were prepared by selective solubilization from ghosts under nondenaturing conditions. We find that the intact ghost has a mean α-helix fraction of 0.37, whereas a low-ionic-strength extract (bands 1, 2, 5, “spectrin”) has a substantially higher helix fraction, 0.55. Further extraction of the ghosts with para-chloromercuribenzoate yields bands 2.1, 4.1, 4.2, and 6; their helix content is only 0.17. Finally, the major intrinsic protein, band 3, was solubilized by a nonionic detergent. Its helix fraction is 0.38.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400040203
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  • 3
    Electronic Resource
    Electronic Resource
    Selective solubilization of proteins from red blood cell membranes by protein perturbants (1973)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 1 (1973), S. 220-232 
    Details
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Isolated human erythrocyte membranes were exposed to a series of reagents known to modify or perturb proteins; these included sodium hydroxide, lithium diiodosalicylate, acid anhydrides, and organic mercurials. Each reagent liberated the same set of relatively polar polypeptides from the membrane, while the other, more hydrophobic species invariably remained associated with the membrane residue. The selective elution pattern was precisely that seen previously with 6 M guanidine hydrocloride. The released polypeptides, comprising half of the membrane protein mass, contained no carbohydrate; current evidence indicates that all of these components are confined to the cytoplasmic surface of the membrane. The residue contained all the lipids and all the glycoproteins. The latter are accessible to the outer membrane surface and, in at least two cases, seem to extend asymmetrically across the thickness of the membrane. Thus, the distinctive elution behavior which defines these two groups of polypeptides relates both to their chemical composition and their organizational disposition in the membrane.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400010307
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