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Am J Physiol Cell Physiol 275: Ca1, 1998;
0363-6143/98 $5.00
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Vol. 275, Issue 3, Ca1-Ca1, September 1998

CORRIGENDA

Volume 269, September 1995 Volume 38, September 1995 

Pages C641-C654: C. M. Fuller, M. S. Awayda, M. P. Arrate, A. L. Bradford, R. G. Morris, C. M. Canessa, B. C. Rossier, and D. J. Benos. "Cloning of a bovine renal epithelial Na+ channel subunit." This article contains two errors in the published sequence of the cDNA alpha bENaC clone presented in Fig. 1. A severe C compression at nucleotide positions 1750 and 1760 resulted in a double frameshift in the C-terminal portion of the sequence. Correction of the nucleotide sequence causes the termination codon to fall at position 1951 (as opposed to position 2092 as previously published), predicting a translated polypeptide of 650 amino acids as opposed to 697 residues as previously reported. This shortened protein has a calculated molecular mass of 73.4 kDa, although it is observed to migrate with an Mr of ~80,000 on 8% SDS-PAGE. The overall homology of the nucleotide sequence with the rat and human alpha ENaC clones is slightly increased by this sequence change to 80% and 84% identities, respectively. In the C terminal region, the identities (similarities) for human/bovine are now 64% (74%) and 55% (68%) for bovine/rat. A revised nucleotide and amino acid sequence is given in Fig. 1. The sites of the C insertion are underlined and the altered amino acid sequence is given in bold. Based on the observation of a major difference in the C-terminus of bovine alpha ENaC (an extra 47 amino acids), we proposed that alpha bENaC was a novel isoform of the ENaC gene family. This conclusion is no longer supported by the present findings. However, this sequence revision does not affect the other data or conclusions of this study. The amended sequence has been deposited with GenBank (Accession U14944). The authors apologize for any inconvenience caused by this error. B. C. Rossier wishes to withdraw his name from the original paper.


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Fig. 1.   Nucleotide and translated amino acid sequence of alpha -bENaC.


Am J Physiol Cell Physiol 275(3):Ca1-Ca1




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