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Primary structure and functional expression of the Na/Ca,K-exchanger from bovine rod photoreceptors.

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Reiländer,  Helmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Achilles,  Anita
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Friedel,  Ute
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Maul,  Gabi
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Lottspeich,  Friedrich
Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society;

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Cook,  Neil J.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Reiländer, H., Achilles, A., Friedel, U., Maul, G., Lottspeich, F., & Cook, N. J. (1992). Primary structure and functional expression of the Na/Ca,K-exchanger from bovine rod photoreceptors. The EMBO Journal, 11(5), 1689-1695. doi:10.1002/j.1460-2075.1992.tb05219.x.


Cite as: http://hdl.handle.net/21.11116/0000-0007-6EED-4
Abstract
Complementary DNA encoding the Na/Ca,K-exchanger was isolated from bovine retina cDNA libraries. The complete full-length cDNA is approximately 4 kb long and contains an open reading frame of 3597 bp. The deduced amino acid sequence corresponds to a protein of 1199 amino acids with a calculated molecular weight of approximately 130 kDa. Hydrophobicity analysis revealed the presence of two alternating sets of hydrophobic and hydrophilic domains. There also exists a hydrophobic region at the N-terminus which may be part of a cleavable signal peptide. The protein shares limited sequence homology with the Na/Ca-exchanger from cardiac sarcolemma. Northern blot analysis indicates that the approximately 6 kb transcript is highly specific for retinal tissue. Insect cells infected with recombinant baculovirus bearing the full-length cDNA express a functional Na/Ca,K-exchanger with an apparent relative molecular weight of approximately 210 kDa, as determined by Western blotting.