Publikation: Stabilization of detergent-solubilized Ca2+ -ATPase by poly(ethylene glycol)
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1989
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Leonhard, Monika
Weltzien, Hans-Ulrich
Restall, Colin
Hall, Christine
Chapman, Dennis
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Biochimica et Biophysica Acta (BBA) - Biomembranes. 1989, 984(2), pp. 193-199. ISSN 0005-2736. Available under: doi: 10.1016/0005-2736(89)90216-2
Zusammenfassung
The (Ca2++Mg2+)-ATPase from sarcoplasmic reticulum (SR) has been solubilized with 1-alkanoyl propanediol 3-phosphorylcholines with chainlengths ranging between 8 and 12 C atoms. A marked dependence of the ATPase activity upon the chainlength was found, indicating that alkyl chainlengths with 12 C atoms are necessary for retention of activity. Addition of poly(ethylene glycol) to the eluting buffers used for gel filtration of the ATPase-detergent micelles was found to increase the activity and the long-term stability significantly. In the presence of Ca2+, the elution volume indicated an ATPase dimer, whereas in the absence of Ca2+ the elution volume indicated a monomeric solution. The purity of the preparations after gel filtration was improved by subsequent chromatography with a hydroxyapatite column.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
ATPase, Ca2+-, enzyme stability, detergent, poly(ethylene glycol), (sarcoplasmic reticulum)
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ISO 690
WELTE, Wolfram, Monika LEONHARD, Kay DIEDERICHS, Hans-Ulrich WELTZIEN, Colin RESTALL, Christine HALL, Dennis CHAPMAN, 1989. Stabilization of detergent-solubilized Ca2+ -ATPase by poly(ethylene glycol). In: Biochimica et Biophysica Acta (BBA) - Biomembranes. 1989, 984(2), pp. 193-199. ISSN 0005-2736. Available under: doi: 10.1016/0005-2736(89)90216-2BibTex
@article{Welte1989Stabi-20875,
year={1989},
doi={10.1016/0005-2736(89)90216-2},
title={Stabilization of detergent-solubilized Ca2+ -ATPase by poly(ethylene glycol)},
number={2},
volume={984},
issn={0005-2736},
journal={Biochimica et Biophysica Acta (BBA) - Biomembranes},
pages={193--199},
author={Welte, Wolfram and Leonhard, Monika and Diederichs, Kay and Weltzien, Hans-Ulrich and Restall, Colin and Hall, Christine and Chapman, Dennis}
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<dcterms:abstract xml:lang="eng">The (Ca2++Mg2+)-ATPase from sarcoplasmic reticulum (SR) has been solubilized with 1-alkanoyl propanediol 3-phosphorylcholines with chainlengths ranging between 8 and 12 C atoms. A marked dependence of the ATPase activity upon the chainlength was found, indicating that alkyl chainlengths with 12 C atoms are necessary for retention of activity. Addition of poly(ethylene glycol) to the eluting buffers used for gel filtration of the ATPase-detergent micelles was found to increase the activity and the long-term stability significantly. In the presence of Ca2+, the elution volume indicated an ATPase dimer, whereas in the absence of Ca2+ the elution volume indicated a monomeric solution. The purity of the preparations after gel filtration was improved by subsequent chromatography with a hydroxyapatite column.</dcterms:abstract>
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