Premium
Primary structure and functional expression of the Na/Ca,K‐exchanger from bovine rod photoreceptors.
Author(s) -
Reiländer H.,
Achilles A.,
Friedel U.,
Maul G.,
Lottspeich F.,
Cook N.J.
Publication year - 1992
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1992.tb05219.x
Subject(s) - biology , complementary dna , microbiology and biotechnology , open reading frame , peptide sequence , amino acid , cdna library , signal peptide , blot , sarcolemma , northern blot , protein primary structure , biochemistry , gene , membrane
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.