The Na,K-ATPase is a transmembrane ion-transporter, extruding three intracellular Na+ ions and importing two extracellular K+ ions per ATPase cycle. The protein is thus involved in maintenance of the electrochemical gradient across the plasma membrane. The ATPase is not only physiologically important for e.g. osmotic regulation, electric excitability and secondary ion transport, but mutations of the ATPase have also been linked to a number of neurological diseases such as RDP and AHC. Using Na,K-ATPase from porcine kidney we aim to establish and optimize protocols for reconstitution of the membrane protein in both liposomes and Saposin-A lipid nanoparticles. The procedure is then to be applied for recombinant enzyme obtained from yeast Picha pastoris for biochemical and structural studies of different isoforms and disease mutants. Activity and thereby the movement of ions by different isoforms and mutants are to be monitored by combining the proteoliposomes with fluorimetry. Preparation of a homogeneus sample of Na,K-ATPase containing Saposin-A lipid nanoparticles are to be pursued, with the purpose of structural studies by electron microscopy.