The carboxy terminus of sodium and potassium ion transporting ATPase is located on the cytoplasmic surface of the membrane.
The carboxy terminus of sodium and potassium ion transporting ATPase is located on the cytoplasmic surface of the membrane.
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转运 ATP 酶的钠离子和钾离子的羧基末端位于膜的细胞质表面。
DOI：
10.1021/bi00062a012
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发表时间：
1993
期刊：
影响因子：
2.9
通讯作者：
Thibault,D
中科院分区：
文献类型：
--
作者：
Thibault,D
1992年12月29日收到的修订稿摘要：绵羊Na+/K+转运ATPase肽QRKIVE中赖氨酸905的质膜位置和绵羊Na+/K+转运ATPase羧基末端RPGGWVEKETYY中赖氨酸1012的位置已被报道分别位于细胞质和胞外[Bayer，R.(1990)BioChemical 29,2551-2256]。我们实验室的这些结果已使用相同程序的扩展进行了重新检查。在存在和不存在皂苷或胆酸盐的情况下，用磷酸吡哆醛和[~3H]硼氢化钠修饰密封的直立囊泡。用金黄色葡萄球菌V8菌株的蛋白酶或胰酶对修饰后的A多肽进行分离和消化，得到两种多肽中的一种。这些消化通过免疫吸附剂，与拜耳使用的相同，针对焦谷氨酰RXIVE或-ETYY。然而，与早期的研究不同的是，在本研究中，从免疫吸附剂中结合和洗脱的修饰的放射性多肽被提交给高效液相，并将它们的各自的迁移率与也用磷酸吡哆醛修饰的合成肽的迁移率进行了比较。以这种方式，正确的、修饰的多肽可以被肯定地鉴定，并且它的特定放射性可以被估计。当胆酸盐被添加到密封的囊泡中时，在修饰之前，赖氨酸1012中的放射性掺入至少增加了3倍，这与该残基的细胞质位置一致。由于用磷酸吡哆醛修饰赖氨酸905残基是困难的，所以不可能确定该残基的位置，但可以表明，Bayer(1990)关于该肽的结论被来自动物质膜(EC 3.6)的污染的、修饰的多肽RYAK(3Hpyr)IV.Na+/K+-转运ATPase[(Na++K+)-ATPase]1的存在所折衷。1.3)是EiE2超家族阳离子转运ATPase的成员，包括内质网钙转运ATPase、钙调蛋白激活ATP酶、质膜钙转运ATPase、胃粘膜H+/K+转运ATPase、真菌H+转运ATPase和植物H+转运ATPase。众所周知，这个超家族的成员都是从一个共同的祖先进化而来的，因此它们在动力学机制、二级、三级和四级结构以及脂双层中的配置方面必须相似(Kyte，1981)。Na+/K+转运ATPase由一个亚基和一个亚基组成(Craig，1982)。/S亚基似乎是(Na++K+)-ATPase和胃粘膜H+/K+-TRANS所独有的。
Revised Manuscript Received December 29, 1992 abstract: The positions, with respect to the plasma membrane, of lysine 905, contained in the peptide QRKIVE, and of lysine 1012, contained in the carboxy-terminal peptide, RPGGWVEKETYY, of ovine Na+/K+-transporting ATPasehave been reported to be cytoplasmic and extracytoplasmic, respectively [Bayer, R.(1990) Biochemistry 29, 2551-2256]. These results from our laboratory have been reexamined using an extension of the same procedure. Sealed right-side-out vesicles were modified with pyridoxal phosphate and sodium [3H] borohydride in the presence and absence of saponin or cholate. The modified a polypeptide was isolated and digested with the proteinase from Staphylococcus aureus strain V8 or trypsin to produce one or the other of these two peptides. These digests were passed over immunoadsorbents, identical to those used by Bayer, directed against pyroglutamylRXIVE or-ETYY. Unlike in the earlier studies, however, in the present studies the modified, radioactive peptides bound and eluted from the immunoadsorbents were submitted to HPLC, and their respective mobilities were compared to those of the synthetic peptides that had also been modified with pyridoxal phosphate. In this manner, the correct, modified peptide could be positively identified, and its specific radioactivity could be estimated. When cholate was added to sealed vesicles, prior to modification, there was at least a 3-fold increase in the incorporation of radioactivity into lysine 1012, consistent with a cytoplasmic location for this residue. It was not possible to determine the position of lysine 905 owing to the difficulty in modifying this residue with pyridoxal phosphate, but it could be shown that the conclusions of Bayer (1990) concerning this peptide were compromised by the presence of a contaminating, modified peptide, RYAK (3Hpyr) IVE.Na+/K+-transporting ATPase [(Na++ K+)-ATPase] 1 from animal plasma membranes (EC 3.6. 1.3) is a member of the EiE2 superfamily of cation-transporting ATPases, which includes endoplasmic reticular Ca2+-transporting ATPase, calmodulin-activated, plasma membrane Ca2+-transporting ATPase, gastric mucosal H+/K+-transporting ATPase, fungal H+-transporting ATPase, and plant H+-transporting ATPase. Members of this superfamily are known to havedescended from a common ancestor and therefore must be similar in their kinetic mechanisms, secondary, tertiary, and quaternary structures, and dispositions in the lipid bilayer (Kyte, 1981). Na+/K+-transporting ATPase consists of one a subunit and one ß subunit (Craig, 1982). The/S subunit seems to be unique to (Na++ K+)-ATPase and gastric mucosal H+/K+-trans-
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与自身免疫性胃炎相关的 60 至 90 kDa 壁细胞自身抗原是胃 H /K( )-ATP 酶（质子泵）的 β 亚基。
DOI：
--
发表时间：
1990
影响因子：
11.1
作者：
B. Toh;P. Gleeson;Richard J. SIMPSONt;Robert L. MORITZt;J. Callaghan;I. Goldkorn;Claerwen M. Jones;T. Martinelli;D. Humphris;J. Pettitt;Yumiko MORIt;Tohru MASUDAt;P. Sobieszczuk;J. Weinstock;T. Mantamadiotis;G. Baldwin
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G. Baldwin
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
发表时间：
1989
影响因子：
3.1
作者：
I. Matthews;J. Colyer;A. M. Mata;N. Green;R. Sharma;A. Lee;J. East
通讯作者：
J. East
影响因子：
1.7
作者：
L. Guo;S. Funakoshi;N. Fujii;H. Yajima
通讯作者：
H. Yajima
膜结合 Na+、K+-ATP 酶暴露域的详细结构分析跨膜排列模型
影响因子：
3.5
作者：
Y. Ovchinnikov;N. M. Arzamazova;E. Arystarkhova;N. M. Gevondyan;N. A. Aldanova;N. Modyanov
通讯作者：
N. Modyanov
脉孢菌质膜 H -ATP 酶的氨基和羧基末端位于细胞质中。
DOI：
--
发表时间：
1989
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Mandala,SM;Slayman,CW
通讯作者：
Slayman,CW