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  • Coupling Factor  (1)
  • disulfide-bonded protein aggregates  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Interaction of a coupling factor from Rhodospirillum rubrum with coupling factor deficient chromatophores (1975)
    Springer
    Archives of microbiology 104 (1975), S. 179-184 
    Details
    ISSN: 1432-072X
    Keywords: Photophosphorylation ; ATP-ase ; Coupling Factor ; Reconstitution ; Rhodospirillum rubrum ; Energy Transduction ; Electron Flow ; Redox Potential
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A coupling factor necessary for the photophosphorylation and Mg2+-ATPase activities of Rhodospirillum rubrum chromatophores has been separated from these particles. Although the redox potential of coupling factor deficient chromatophores is slightly more oxidized than of the control, the addition of the coupling factor for reconstitution does not alter the redox potential. Phenazine methosulfate cannot restore or significantly enhance the photophosphorylation activities of uncoupled or reconstituted chromatophores compared to the control. The coupling factor can bind to coupling factor deficient membranes without addition of magnesium ions and thus restore the photophosphorylation and Mg2+-ATPase activities of these vesicles. The Ca2+-ATPase in the coupling factor preparation shows binding characteristics similar to those of the coupling factor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00447321
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  • 2
    Electronic Resource
    Electronic Resource
    Vesicles isolated from ATP-depleted erythrocytes and out of thrombocyte-rich plasma (1978)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 8 (1978), S. 375-389 
    Details
    ISSN: 0091-7419
    Keywords: thrombocyte-rich plasma ; disulfide-bonded protein aggregates ; erythrocyte fragmentation ; human erythrocytes ; in vitro aging ; ATP-depletion ; spectrin-free vesicles ; fragments of erythrocytes ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: When human erythrocytes are depleted of endogenous ATP they release spectrin-free vesicles as a light vesicle fraction [Lutz et al: J Cell Biol 73:548, 1977] and chains of rounded vesicles as well as flattened myelin forms in a heavy vesicle fraction. The heavy fraction retains some spectrin, and glycophorin is partially degraded. The release of both types of fragments is not dependent upon added Ca+2, and 50 μM EGTA does not prevent the vesicle release. Concomitant with vesicle release, a large fraction of the major protein components of the cell is found in disulfide-bonded aggregates.A protocol is outlined to recover erythrocyte-specific fragments from thrombocyte-rich plasma. It allows detection of spectrin-free vesicles in whole blood stored under blood bank conditions for 12 days. In freshly drawn blood no such vesicles are observed, but particles are obtained that are different from thrombocyte fragments and that show a prominent glycoprotein running slightly faster than glycophorin.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400080314
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