Evidence for the cytoplasmic location of the N- and C-terminal segments of sarcoplasmic reticulum (Ca2+-Mg2+)-ATPase.
Evidence for the cytoplasmic location of the N- and C-terminal segments of sarcoplasmic reticulum (Ca2+-Mg2+)-ATPase.
复制标题
肌浆网 (Ca2 -Mg2 )-ATP 酶 N 端和 C 端片段在细胞质中定位的证据。
DOI：
10.1016/0006-291x(89)92653-3
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发表时间：
1989
影响因子：
3.1
通讯作者：
J. East
中科院分区：
文献类型：
--
作者：
I. Matthews;J. Colyer;A. M. Mata;N. Green;R. Sharma;A. Lee;J. East
针对5个肽产生抗体，所述5个肽对应于快收缩兔骨骼肌肌浆网（SR）的（Ca ~（2+）→ Mg ~（2+））-ATP酶的片段，包括N-和C-末端区域。除了针对对应于残基567-582的肽的抗体之外，所有抗体都与完整SR囊泡中的ATP酶强烈结合，表明表位位于SR的细胞质面上。当囊泡被破坏时，通过在SDS中溶解，这些抗体的结合没有改变，这是首次证实SR（Ca ~（2+）→ Mg ~（2+））-ATPase的N-和C-末端区域的位置。这些意见进行了讨论，在目前的结构模型的ATP酶。
Antibodies were produced against 5 peptides corresponding to segments of the (Ca2+Mg2+)-ATPase of fast-twitch rabbit skeletal muscle sarcoplasmic reticulum (SR) including the N- and C-terminal regions. With the exception of antibodies directed against the peptide corresponding to residues 567–582 all antibodies boud strongly to the ATPase in intact SR vesicles, indicating that the epitopes were located on the cytoplasmic face of the SR. When the vesicles were disrupted, by solubilisation in SDS, binding of these antibodies was unchanged, further supporting the idea that these epitopes were located on the cytoplasmic face of SR. This is the first demonstration of the location of the N- and C-terminal regions of SR (Ca2+Mg2+)-ATPase. These observations are discussed in the light of current structural models of the ATPase.