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Deformation behavior of erythrocyte ghost
Biopolymers, 1969AbstractBiological membranes consist mainly of lipids and proteins. At present, the structure of the lipid phase appears to be established, but hypotheses on the molecular organization of the protein are difficult to support. Thus the deformation behavior of whole human erythrocyte ghosts, ghosts after the selective removal of lipids and ghosts ...
J J, Blais, P H, Geil
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Phospholipid asymmetry in human erythrocyte ghosts
Journal of Cellular Physiology, 1985AbstractUsing phospholipase digestion and the fluorescent probe merocyanine 540 the maintenance of phospholipid asymmetry in the plasma membrane of human erythrocyte ghosts was investigated. Digestion with phospholipase A2 indicated that ghosts prepare in the presence of Mg++ as the only divalent cation retained the normal phospholipid asymmetry ...
P, Williamson +4 more
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The preparation of nucleated erythrocyte ghosts from avian erythrocytes
British Poultry Science, 1971Synopsis A method is described for the preparation of erythrocyte ghosts, which are haemoglobin‐depleted, from domestic fowl and turkey erythrocytes. These erythrocyte ghosts retain their ellipsoid shape and their nuclei, which are shown to possess the typical double nuclear membrane. In the cytoplasmic compartment of the ghosts, mitochondria have been
J R, Harris, J N, Brown
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The Journal of Membrane Biology, 1989
A model for the binding of 5-nitroxide stearate, I(12.3), to human erythrocyte ghosts was developed by comparing spin probe interactions with ghosts and liposomes prepared from ghosts. At low probe/lipid (P/L less than 1/2500), I(12.3) binds to a similar class of high-affinity, noninteracting sites in both ghosts and liposomes, indicating that lipid ...
L M, Gordon, F D, Looney, C C, Curtain
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A model for the binding of 5-nitroxide stearate, I(12.3), to human erythrocyte ghosts was developed by comparing spin probe interactions with ghosts and liposomes prepared from ghosts. At low probe/lipid (P/L less than 1/2500), I(12.3) binds to a similar class of high-affinity, noninteracting sites in both ghosts and liposomes, indicating that lipid ...
L M, Gordon, F D, Looney, C C, Curtain
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The size of erythrocyte ghosts
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1981The volume of resealed erythrocyte ghosts formed during hypotonic hemolysis of normal human erythrocytes was measured by means of a continuous mean corpuscular volume analyzer. The final volume of resealed ghosts was 140.6 +/- 15.2 fl. Strong correlations exist between the volume of ghosts and the initial mean corpuscular volume and mean corpuscular ...
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PHOTOCHEMICAL PROPERTIES OF ERYTHROCYTE GHOSTS CONTAINING PORPHYRIN
Photochemistry and Photobiology, 1988Abstract— Rabbit erythrocyte cell ghosts were prepared containing tetrasodium meso‐tetra (4‐sulfona‐to‐phenyl) porphine (12‐hydrate), a water soluble porphyrin. Laser flash kinetic spectroscopy of the suspension revealed a difference spectrum consistent with the porphyrin T, state.
P A, Firey, M A, Rodgers
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Calcium efflux from human erythrocyte ghosts
The Journal of Membrane Biology, 1970The passive Ca efflux from human red cell ghosts was studied in media of differing ion compositions and compared to the ATP-dependent Ca efflux. Cells were loaded with(45)Ca during reversible hemolysis, and the loss of radioactivity into the non-radioactive incubation medium was measured, usually for 3 hr at 37°C. Analysis of the efflux curves revealed
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Metabolism of deoxyinosine by human erythrocyte ghosts
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1966Abstract Deoxyinosine was metabolized by human erythrocyte ghosts. Kinetic studies revealed an accumulation of hypoxanthine, a decrease in deoxypentose, and an initial uptake of inorganic phosphate followed by its eventual release. Intermediates of the pathway identified were triose phosphate (glyceraldehyde 3-phosphate and dihydroxyacetone phosphate)
F J, Lionetti, N L, Fortier
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Baboon erythrocyte ghosts contain beta-adrenergic receptors
American Journal of Physiology-Cell Physiology, 1985We have used the beta-adrenergic antagonist [3H]dihydroalprenolol [( 3H]DHA) to identify binding sites on the erythrocyte membrane of the primate Papio ursinus. Analysis of the saturation isotherm revealed binding to be saturable with a maximal number of binding sites of 499 fmol/mg protein. [3H]DHA binds specifically to the erythrocyte ghosts with an
E E, Susanni +3 more
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