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  • 1
    Electronic Resource
    Electronic Resource
    The band 3-rich membrane of llama erythrocytes: Studies on cell shape and the organization of membrane proteins (1983)
    Springer
    The journal of membrane biology 72 (1983), S. 161-171 
    Details
    ISSN: 1432-1424
    Keywords: erythrocytes ; membranes ; llama ; organization ; proteins ; band 3 ; cell shape ; deformability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The erythrocyte membrane of the llama was characterized in comparison to that of the human. The llama erythrocyte was an elliptical disk that resisted shape alterations in hyperosmotic buffers and following metabolic depletion, both of which induce spiculation of the human red cell. Lysophosphatidylcholine incorporation produced minor serrations of the edge of the llama disk but no spicules, whereas human red cells became sphero-echinocytes. The polypeptide profiles in the membranes of the two species were similar, except for several noteworthy differences: a marked elevation in the relative content of band 3; the absence of membrane-bound band 6; and simpler glycoprotein pattern in the llama. The concentration of band 3 in llama was about two and a half to three times that in the human and intramembrane particles in the protoplasmic leaflet of freeze-fractured llama membrane were correspondingly increased. The selective solubilization of bands 1, 2 and 5 in low ionic strength buffer, and all of the peripheral proteins in high alkaline buffer were similar except for increased retention of ankyrin by the llama membrane. These data suggest a similar disposition of membrane proteins. The llama membrane was markedly resistant to the solubilization of integral proteins by the nonionic detergent, Triton X-100. This property and the general resistance to shape changes may be related to the high concentration of band 3.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01870583
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  • 2
    Electronic Resource
    Electronic Resource
    Shape determinants of McLeod acanthocytes (1989)
    Springer
    The journal of membrane biology 107 (1989), S. 213-218 
    Details
    ISSN: 1432-1424
    Keywords: acanthocytes ; bilayer ; cell shape ; chlorpromazine ; erythrocytes ; lipid ; McLeod ; membranes ; organization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary We have sought to elucidate the spiculated shape of McLeod erythrocytes. Red cells from a normal donor and from a McLeod patient were incubated in phosphate-buffered saline containing 0, 0.05, or 0.1mm chlorpromazine at 0°C for 5 min. then glutaraldehyde-fixed, and examined by scanning electron microscopy. The normal red cells were biconcave disks in which chlorpromazine induced inward (negative) curvature: deep cupping (stomatocytosis) and multiple invaginations. The McLeod cells were mostly spiculated. Chlorpromazine at lower concentration converted them into biconcave disks and, at higher concentration, into stomatocytes. These results support the hypothesis that the spiculation of McLeod cells is the result of an imbalance of surface area between the two lipid leaflets of the membrane; that is, a bilayer couple effect. We determined the numerical density of intramembrane particles (IMP) in replicas of both fracture faces of red cells subjected to freeze fracture and rotary shadowing. These values were as follows (expressed per μm2 of membrane ±sd): the normal protoplasmic fracture face had 2200±306 and the McLeod had 2300±250. The normal exoplasmic fracture face had 388±75 and the McLeod had 330±59. We conclude that there is no evidence for derangement of band 3, the principal protein in theIMP, in McLeod erythrocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871936
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  • 3
    Electronic Resource
    Electronic Resource
    Fine structure of the band 3 protein in human red cell membranes: Freeze-fracture studies (1978)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 8 (1978), S. 325-335 
    Details
    ISSN: 0091-7419
    Keywords: band 3 protein ; freez-fracture electron microscopy ; glyceraldehyde-3 phosphate dehydrogenase ; integral membrane protein ; intramembrane particle ; membrane proteins, unmasking ; spectrin ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The major red cell membrane protein, band 3, is a glycoprotein which extends across the membrane from the extracellular space into the cytoplasmic compartment. It is widely held that band 3 is a component of the intramembrane particles (IMP) which can be demonstrated by freeze-fracture electron microscopy. In this study, we find that the outer surface poles of the IMP can be seen by freeze-etching after they are unmasked by proteolysis under conditions which excise the surrounding sialopeptides from the membrane. The poles appear as distinctive projections, 30-50 Å in diameter, the “ES particles.” The ES particles remain associated with the outer surface of the membrane following cleavage of the band 3 polypeptide by chymotrypsin or pronase. This is consistent with previous biochemical studies which have shown that the 38,000-dalton outer surface segment of band 3 is intercalated in the lipid bilayer. A granulofibrillar component at the inner surface of the membrane is provisonally identified as the 40,000-dalton inner-surface domain of band 3.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400080310
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    Paper (German National Licenses)
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