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  • liposome stability  (1)
  • rabbit muscle  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 120 (1993), S. 119-126 
    ISSN: 1573-4919
    Keywords: liposome stability ; liposome-blood interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Lipid composition and specially their electrostatic properties, were found to greatly influence the stability of liposomes in human blood serum. The amount and type of serum proteins bound to the liposomes were also clearly influenced by lipid composition and charge of liposomes. a good correlation was found between the amount of serum proteins adsorbed to a given type of liposome and its instability as measured by the release of an encapsulated fluorescent probe. Liposomes that bind the highest amount of protein were the least stable, except for the case of liposomes containing gangliosides, which were fairly stable even at a high amount of bound protein. Liposomes with neutral charge containing phosphatidylcholine were the most stable and bound the lowest amount of protein. Liposomes with positive charge behaved similarly to those with neutral charge. However, the stability of negatively charged liposomes was very dependent on their composition. Those liposomes containing only one class of negatively charged phospholipids bound a great amount of protein and were very unstable. However, those liposomes containing also phosphatidylcholine bound less protein and were more stable. The examination of the electrophoresis patterns of serum proteins bound to the different types of liposomes indicated the presence of specific proteins which correlated with liposome instability. (Mol Cell Biochem120: 119–126, 1993)
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    ISSN: 1573-6881
    Keywords: H+ flux ; K+ flux ; Ca2+-pump ; sarcoplasmic reticulum ; rabbit muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The release of H+ during the oxalate-supported Ca2+ uptake in sarcoplasmic reticulum vesicles is kinetically coincident with the initial phase of Ca2+ accumulation. The Ca2+ uptake is increased and the H+ release is decreased in the presence of KCl and other monovalent chloride salts as expected for a H+-monovalent cation exchange. The functioning of the Ca2+-pump is disturbed by the presence of potassium gluconate and, to a lesser extent, of choline chloride. These salts do not inhibit the ATPase activity of Ca2+-permeable vesicles, suggesting a charge imbalance inhibition which is specially relevant in the case of gluconate. Therefore, K+, and also Cl−, appear to be involved in secondary fluxes during the active accumulation of Ca2+. The microsomal preparation seems homogeneous with respect to the K+-channel, showing an apparent rate constant for K+ release of approximately 25 s−1 measured with the aid of86Rb+ tracer under equilibrium conditions. A Rb+ efflux, sensitive to Ca2+-ionophore, can be also detected during the active accumulation of Ca2+. The experimental data suggest that both monovalent cations and anions are involved in a charge compensation during the Ca2+ uptake and H+ release. Fluxes of these highly permeable ions would contribute to cancel the formation of a resting membrane potential through the sarcoplasmic reticulum membrane.
    Type of Medium: Electronic Resource
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