| Literature DB >> 9704004 |
Y Shima1, Y Tada, M Furuki, Y Hara, H Ohta.
Abstract
The Na+,K(+)-ATPase activity of membranes from a behavioral mutant of C. elegans was found to be about one-third that of the wild-type. The levels of mRNA and polypeptide of Na+,K(+)-ATPase alpha-subunit in the mutant were as high as those in the wild-type, but the level of the phosphorylated intermediate of the Na+,K(+)-ATPase in the mutant worm was 80% lower than that in the wild-type. A single predicted amino acid replacement (Leu to Phe) was found in a highly conserved region in the alpha-subunit that is involved in the formation of phosphorylated intermediate. The abnormal feeding behavior of the mutant worm may be attributed to this missense mutation.Entities:
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Year: 1998 PMID: 9704004 DOI: 10.1006/bbrc.1998.8981
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575