論文 - 詳細
| RRC ID | 49626 |
|---|---|
| 著者 | Homareda H, Otsu M, Yamamoto S, Ushimaru M, Ito S, Fukutomi T, Jo T, Eishi Y, Hara Y. |
| タイトル | A possible mechanism for low affinity of silkworm Na+/K+-ATPase for K. |
| ジャーナル | J Bioenerg Biomembr |
| Abstract |
The affinity for K+ of silkworm nerve Na+/K+-ATPase is markedly lower than that of mammalian Na+/K+-ATPase (Homareda 2010). In order to obtain clues on the molecular basis of the difference in K+ affinities, we cloned cDNAs of silkworm (Bombyx mori) nerve Na+/K+-ATPase α and β subunits, and analyzed the deduced amino acid sequences. The molecular masses of the α and β subunits were presumed to be 111.5 kDa with ten transmembrane segments and 37.7 kDa with a single transmembrane segment, respectively. The α subunit showed 75% identity and 93% homology with the pig Na+/K+-ATPase α1 subunit. On the other hand, the amino acid identity of the β subunit with mammalian counterparts was as low as 30%. Cloned α and β cDNAs were co-expressed in cultured silkworm ovary-derived cells, BM-N cells, which lack endogenous Na+/K+-ATPase. Na+/K+-ATPase expressed in the cultured cells showed a low affinity for K+ and a high affinity for Na+, characteristic of the silkworm nerve Na+/K+-ATPase. These results suggest that the β subunit is responsible for the affinity for K+ of Na+/K+-ATPase. |
| 巻・号 | 49(6) |
| ページ | 463-472 |
| 公開日 | 2017-12-1 |
| DOI | 10.1007/s10863-017-9729-5 |
| PII | 10.1007/s10863-017-9729-5 |
| PMID | 29047027 |
| MeSH | Amino Acid Sequence Animals Bombyx / enzymology* DNA, Complementary Potassium / metabolism* Protein Binding Protein Subunits / metabolism Protein Subunits / physiology Sodium-Potassium-Exchanging ATPase / chemistry* Sodium-Potassium-Exchanging ATPase / metabolism |
| IF | 2.524 |
| 引用数 | 0 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 1 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| カイコ | p20 |
| ヒト・動物細胞 | BM-N(RCB0457) |