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  • LUBBERDING, Henk J.  (2)
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  • 1
    Online Resource
    Online Resource
    Characterization of reconstituted ATPase complex proteoliposomes prepared from the thermophilic cyanobacterium Synechococcus 6716
    Wiley ; 1983
    In:  European Journal of Biochemistry Vol. 137, No. 1-2 ( 1983-12), p. 101-106
    Details
    In: European Journal of Biochemistry, Wiley, Vol. 137, No. 1-2 ( 1983-12), p. 101-106
    Abstract: The preparation and some properties are described of proteoliposomes consisting of the ATPase complex and lipids from the thermophilic cyanobacterium Synechococcus 6716. In the proteoliposomes (about 200 nm in diameter) only a low amount of protein can be incorporated (protein/lipid ratio of 0.01 w/w) and they show very few protein particles on freeze‐fracture replicas. The octyl glucoside and cholate dialysis method of reconstitution yielded stable proteoliposomes with a relatively low proton permeability. ATP hydrolysis and 32 P i /ATP exchange activities were about 400 and 120nmol · min −1 · mg protein −1 , respectively; the former was strongly stimulated by an uncoupler. ATP hydrolysis induces membrane energization as monitored by membrane‐potential‐ and surface‐potential‐indicating probes and by different pH indicators trapped inside the vesicles. The probes used were a membrane‐bound fluorescent aminoacridine, which monitors surface charge‐density changes, the native carotenoids and added oxonol VI for monitoring electrical potential in the membrane and the pH indicators neutral red and cresol red. The different rise kinetics of these probes indicate that proton accumulation upon ATP hydrolysis involves at least two steps: a membrane‐localized potential charge and proton transfer followed by a much slower acidification of the bulk intravesicular space. Internal neutral red and cresol red seem to discriminate between proton translocation to the internal interface and bulk space, respectively.
    Type of Medium: Online Resource
    ISSN: 0014-2956 , 1432-1033
    URL: Issue
    URL: Article
    DOI: 10.1111/ejb.1983.137.issue-1-2
    DOI: 10.1111/j.1432-1033.1983.tb07801.x
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1983
    detail.hit.zdb_id: 1398347-7
    detail.hit.zdb_id: 2172518-4
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 2
    Online Resource
    Online Resource
    Isolation, purification and characterization of the ATPase complex from the thermophilic cyanobacterium Synechococcus 6716
    Wiley ; 1983
    In:  European Journal of Biochemistry Vol. 137, No. 1-2 ( 1983-12), p. 95-99
    Details
    In: European Journal of Biochemistry, Wiley, Vol. 137, No. 1-2 ( 1983-12), p. 95-99
    Abstract: The ATPase complex is isolated and purified from membrane vesicles of the thermophilic cyanobacterium Synechococcus 6716 by octyl glucoside and cholic acid by a modification of the procedure for its extraction from spinach chloroplasts. The complex is purified by differential centrifugation and ammonium sulfate precipitation and by gel filtration on Sepharose 6B. The purified fraction, without any phycocyanin contamination, shows ATP hydrolysis activity and P i /ATP exchange activity of 1564 and 350 nmol · min −1 · mg protein −1 , respectively. N , N′ ‐Dicyclohexylcarbodiimide inhibits the ATP hydrolysis activity of this purified fraction. On polyacrylamide gels most typical F 1 ATPase polypeptides are identified, but the low‐molecular weight polypeptides visible cannot be ascribed to the F o part of the complex with certainty; non‐identified bands around 30kDa are also present.
    Type of Medium: Online Resource
    ISSN: 0014-2956 , 1432-1033
    URL: Issue
    URL: Article
    DOI: 10.1111/ejb.1983.137.issue-1-2
    DOI: 10.1111/j.1432-1033.1983.tb07800.x
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1983
    detail.hit.zdb_id: 1398347-7
    detail.hit.zdb_id: 2172518-4
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
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