Poly A sequences at the 3' termini of rabbit globin mRNAs.
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Biomedical subjects
Publications and source records attributed to J B Lingrel.
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We have isolated and characterized a complementary DNA for the catalytic subunit of the sheep kidney sodium/potassium-dependent ATPase. The 1,016-amino-acid protein seems to have eight transmembrane domains. The apparent ouabain binding site is located at the extracellular junction of two transmembrane domains and is linked to the phosphorylation site by a 60-amino-acid conserved sequence that may be a major channel for energy transduction.
The sodium/potassium-dependent ATPase [(Na+ + K+)ATPase], which establishes and maintains the Na+ and K+ gradients across the plasma membrane of animal cells, consists of two subunits, alpha and beta. Complementary DNA clones encoding the catalytic (alpha) subunit of sheep kidney and Torpedo californica electroplax enzymes have previously been isolated and characterized. However, there is little information concerning the primary structure of the beta-subunit, a glycoprotein of unknown function and relative molecular mass (Mr) approximately 55,000 (ref. 3). Here we describe the isolation and characterization of a cDNA clone containing the entire coding region of the beta-subunit of the sheep kidney (Na+ + K+)ATPase. We also discuss structural aspects of the protein and present evidence for a possible evolutionary relationship with the KdpC subunit of the Escherichia coli K+-ATPase.
We mapped the beta-globin gene cluster of the goat (Capra hircus) to a specific chromosomal region of the species, using in situ hybridization. The probe we used was a 1.2-kb Eco RI/Bam HI genomic DNA fragment that was 3H labeled to high specific activity by the random primer method. This DNA fragment contains part of the 5' flanking region and the first two exons of the epsilon IV gene of the goal beta-globin gene cluster. Our results show that this gene cluster is on chromosome 7 in the region of bands 33 to 35 based on BrdU G-banded chromosome preparations of this species.
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