Stabilization of detergent-solubilized Ca2+ -ATPase by poly(ethylene glycol)
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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.
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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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