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  • Title: Bulk properties of the lipid bilayer are not essential for the thermal stability of Na,K-ATPase from shark rectal gland or pig kidney.
    Author: Hansen AS, Kraglund KL, Fedosova NU, Esmann M.
    Journal: Biochem Biophys Res Commun; 2011 Mar 25; 406(4):580-3. PubMed ID: 21352812.
    Abstract:
    The thermal stability of Na,K-ATPase from pig kidney is markedly greater than that of Na,K-ATPase from shark salt glands. The role of the lipid bilayer is studied by solubilisation of the membrane-bound enzyme in the nonionic detergent octaethyleneglycoldodecylmonoether (C(12)E(8)), addition of excess dioleylphosphatidylcholine (DOPC) or palmitoyloleylphosphatidylcholine (POPC) and reconstitution of membranes by removal of detergent. At 54°C the reconstituted enzymatically active pig enzyme retains a high thermal stability, and reconstituted shark enzyme retains a low thermal stability, even with a 9-fold excess of DOPC. This result suggests that the origin of the difference in thermal stability is not related to bulk lipid properties of the native membranes.
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