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  • 1
    Electronic Resource
    Electronic Resource
    Interaction of europium(III) with phospholipid vesicles as monitored by laser-excited europium(III) luminescence (1986)
    s.l. : American Chemical Society
    Biochemistry 25 (1986), S. 5834-5838 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00367a074
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Lysophospholipid-mediated alterations in the calcium transport systems of skeletal and cardiac muscle sarcoplasmic reticulum (1988)
    Springer
    Molecular and cellular biochemistry 79 (1988), S. 81-89 
    Details
    ISSN: 1573-4919
    Keywords: calcium transport ; sarcoplasmic reticulum ; lysophospholipids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The effects of various lysophospholipids on the calcium transport activity of sarcoplasmic reticulum (SR) from rabbit skeletal and canine cardiac muscles were examined. The lipids decreased calcium transport activity in both membrane types; the effectiveness being in the order lysoPC 〉 lsyoPS, lysoPG 〉 lysoPE. The maximum inhibition induced by lysoPC, lysoPG and lysoPS was greater than 85% of the normal Ca2+-transport rate. In cardiac SR lysoPE had a maximal inhibition of about 50%. Half maximal inhibition of calcium transport by lysoPC was achieved at 110 nmoles lysoPC/mg SR. At this concentration of lysoPC, the (Ca2+ + Mg2+)-ATPase and Ca2+-uptake activities were inhibited to the same extent (about 60%) in skeletal sarcoplasmic reticulum, while in cardiac sarcoplasmic reticulum, there was less than 20% inhibition of the Ca2+ + Mg2+-ATPase activity. Studies with EGTA-induced passive calcium efflux showed that up to 200 nmoles lysoPC/mg SR did not alter calcium permeability significantly in cardiac sarcoplasmic reticulum. In skeletal muscle membranes the lysophospholipid mediated decrease in calcium uptake correlated well with the increase in passive calcium efflux due to lysophosphatidylcholine. The difference in the lysophospholipid-induced effects on the sarcoplasmic reticulum from the two muscle types probably reflects variations in protein and other membrane components related to the respective calcium transport systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00229401
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  • 3
    Electronic Resource
    Electronic Resource
    Regulation of cardiac sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase (1988)
    Springer
    Molecular and cellular biochemistry 82 (1988), S. 45-49 
    Details
    ISSN: 1573-4919
    Keywords: sarcoplasmic reticulum ; Ca2+-binding sites ; Ca2+-ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The two high affinity calcium binding sites of the cardiac (Ca2+ + Mg2+)-ATPase have been identified with the use of Eu3+. Eu3+ competes for the two high affinity calcium sites on the enzyme. With the use of laser-pulsed fluorescent spectroscopy, the environment of the two sites appear to be heterogeneous and contain different numbers of H2O molecules coordinated to the ion. The ion appears to be occluded even further in the presence of ATP. Using non-radiative energy transfer studies, we were able to estimate the distance between the two Ca2+ sites to be between 9.4 to 10.2 A in the presence of ATP. Finally, from the assumption that the calcium site must contain four carboxylic side chains to provide the 6–8 ligands needed to coordinate calcium, and based on our recently published data, we predict the peptidic backbone of the two sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00242514
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  • 4
    Electronic Resource
    Electronic Resource
    Estimation of inter-binding-site distances in sarcoplasmic reticulum (Ca2+ + Mg2+)ATPase under occluded and non-occluded conditions (1988)
    Springer
    Molecular and cellular biochemistry 82 (1988), S. 55-58 
    Details
    ISSN: 1573-4919
    Keywords: calcium binding ; sarcoplasmic reticulum ; europium luminescence ; energy transfer ; chromium-ATP ; calcium occlusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Distances between binding sites in skeletal sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase were estimated by measuring energy transfer between a luminescent lanthanide probe for the calcium sites (Eu3+) and suitable acceptors. A distance measurement between the two calcium binding sites of the enzyme was made with and without MgATP, corresponding to two different states in the hydrolytic cycle. We found that without ATP, the inter-calcium-site distance is about 0.9 nm, while in the presence of MgATP these sites are 0.05 nm to 0.1 nm closer. We also estimated the distance from the calcium sites to the hydrolytic site using CrATP as an acceptor; this distance is approximately 1.8 nm. These measurements provide the start for a description of intramolecular movement during the transport cycle, and should be of use in mapping out the three-dimensional structure of the Ca2+ pump.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00242516
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    Paper (German National Licenses)
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