Ohta T, Yoshida M, Nagano K, Hirano H, Kawamura M
FEBS Lett. 1986 Aug 18;204(2):297-301. doi: 10.1016/0014-5793(86)80832-8.
Membrane bound dog kidney (Na,K)-ATPase was digested with trypsin. The peptides that were recovered in the supernatant were purified and sequenced. By comparing these results with the sequence of alpha- and human beta-subunits, the location of each of the peptides could be allotted. Both accessibility to trypsin and the facility of release into the water phase indicated that these peptides were derived from the exposed surface of the intact enzyme. The sequence, GXGXXG, reported in the Torpedo californica beta-subunit [(1986) FEBS Lett. 196, 315-319] was likely a mere coincidence with the sequence of the dinucleotide-binding site, since the last glycine was replaced by proline in the sequence of the dog beta-subunit. A disulfide bridge was found within a peptide derived from the beta-subunit. A possible model for the beta-subunit structure is proposed.
用胰蛋白酶消化膜结合的犬肾（钠，钾）-ATP酶。回收上清液中的肽段并进行纯化和测序。通过将这些结果与α亚基和人β亚基的序列进行比较，可以确定每个肽段的位置。对胰蛋白酶的可及性以及释放到水相中的难易程度均表明，这些肽段源自完整酶的暴露表面。在加州电鳐β亚基中报道的序列GXGXXG[（1986年）欧洲生物化学学会联合会快报。196, 315 - 319]可能只是与二核苷酸结合位点的序列巧合，因为在犬β亚基的序列中最后一个甘氨酸被脯氨酸取代。在源自β亚基的一个肽段中发现了一个二硫键。提出了β亚基结构的一个可能模型。
