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On the mechanism of Na plus and K plus-stimulated hydrolysis of adenosine triphosphate. 2. Comparison of nucleotide specificities of Na plus and K plus-activated ATPase and Na plus-dependent phosphorylation of cell membranes.

作者信息

Schoner W, Beusch R, Kramer R

出版信息

Eur J Biochem. 1968 Dec;7(1):102-10. doi: 10.1111/j.1432-1033.1968.tb19580.x.

DOI:10.1111/j.1432-1033.1968.tb19580.x
PMID:4237210
Abstract
摘要

相似文献

1
On the mechanism of Na plus and K plus-stimulated hydrolysis of adenosine triphosphate. 2. Comparison of nucleotide specificities of Na plus and K plus-activated ATPase and Na plus-dependent phosphorylation of cell membranes.论钠钾离子刺激下三磷酸腺苷水解的机制。2. 钠钾离子激活的三磷酸腺苷酶的核苷酸特异性与细胞膜的钠依赖性磷酸化作用的比较
Eur J Biochem. 1968 Dec;7(1):102-10. doi: 10.1111/j.1432-1033.1968.tb19580.x.
2
Relationships between erythrocyte membrane phosphorylation and adenosine triphosphate hydrolysis.红细胞膜磷酸化与三磷酸腺苷水解之间的关系。
J Biol Chem. 1968 Apr 25;243(8):1957-65.
3
Comparison of some minor activities accompanying a preparation of sodium-plus-potassium ion-stimulated adenosine triphosphatase from pig brain.猪脑钠钾离子刺激的三磷酸腺苷酶制备过程中一些次要活动的比较。
Biochem J. 1968 Jan;106(1):113-21. doi: 10.1042/bj1060113.
4
C14-ADP-ATP exchange activity and the Na+, K+-stimulated ATPase system.C14-ADP-ATP交换活性与钠钾刺激的ATP酶系统。
Arch Biochem Biophys. 1967 Apr;120(1):230-1. doi: 10.1016/0003-9861(67)90621-2.
5
[Mode of action of sodium on the phosphorylation of "Mg 2+ -Na + -K + -dependent" ATPase of human erythrocyte membranes].[钠对人红细胞膜“Mg²⁺ - Na⁺ - K⁺依赖性”ATP酶磷酸化作用的机制]
C R Acad Hebd Seances Acad Sci D. 1971 Sep 13;273(11):982-4.
6
Demonstration of a phosphopeptide intermediate in the Mg ++ -dependent, Na + - and K + -stimulated adenosine triphosphatase reaction of the erythrocyte membrane.红细胞膜镁离子依赖、钠离子和钾离子刺激的三磷酸腺苷酶反应中磷酸肽中间体的证实。
Proc Natl Acad Sci U S A. 1972 May;69(5):1216-20. doi: 10.1073/pnas.69.5.1216.
7
(Na+-K+)-activated ATPase in cattle erythrocytes.牛红细胞中的(钠 - 钾)激活的ATP酶
Biochim Biophys Acta. 1974 Sep 23;363(3):397-403. doi: 10.1016/0005-2736(74)90078-9.
8
The role of bound potassium ions in the hydrolysis of low concentrations of adenosine triphosphate by preparations of membrane fragments from ox brain cerebral cortex.结合钾离子在牛脑大脑皮质膜碎片制剂水解低浓度三磷酸腺苷中的作用。
Biochem J. 1970 Nov;120(1):15-24. doi: 10.1042/bj1200015.
9
Phosphorylation of bovine brain Na + , K + -stimulated ATP phosphohydrolase by adenosine ( 32 P)triphosphate studied by a rapid-mixing technique.通过快速混合技术研究腺苷(32P)三磷酸对牛脑钠钾激活的ATP磷酸水解酶的磷酸化作用。
Biochim Biophys Acta. 1972 Jan 17;255(1):231-8. doi: 10.1016/0005-2736(72)90025-9.
10
Kinetics of (Na + ,K + )-ATPase of human erythrocyte membranes. I. Activation by Na + and K + .人红细胞膜(钠+,钾+)-ATP酶的动力学。I. 钠和钾的激活作用
Biochim Biophys Acta. 1972 Dec 1;290(1):300-9. doi: 10.1016/0005-2736(72)90072-7.

引用本文的文献

1
Computer modelling reveals new conformers of the ATP binding loop of Na/K-ATPase involved in the transphosphorylation process of the sodium pump.计算机建模揭示了参与钠泵转磷酸化过程的钠钾ATP酶ATP结合环的新构象。
PeerJ. 2017 Mar 14;5:e3087. doi: 10.7717/peerj.3087. eCollection 2017.
2
Brain capillary guanosine triphosphatase: a distinction from adenosine triphosphatase.脑毛细血管鸟苷三磷酸酶:与腺苷三磷酸酶的区别。
Experientia. 1980 Jan 15;36(1):40-2. doi: 10.1007/BF02003958.
3
The relationship between ATP and an electrogenic pump in the plasma membrane of Neurospora crassa.
粗糙脉孢菌质膜中ATP与生电泵之间的关系。
J Membr Biol. 1973;14(4):305-38. doi: 10.1007/BF01868083.
4
The relationship of the (Na + + K + )-activated enzyme system to transport of sodium and potassium across the cell membrane.(钠++钾+)激活酶系统与钠和钾跨细胞膜转运的关系。
J Bioenerg. 1973 Jan;4(1):1-30. doi: 10.1007/BF01516049.
5
Separation at neural pH of a 32P-labelled membrane protein associated with the sodium-plus-magnesium ion-activated adenosine triphosphatase from ox brain.在神经pH值下,从牛脑中分离出与钠加镁离子激活的三磷酸腺苷酶相关的32P标记膜蛋白。
Biochem J. 1970 Oct;119(5):44P-45P. doi: 10.1042/bj1190044p.
6
The effect of chemical agents on the turnover of the bound phosphate associated with the sodium-and-potassium ion-stimulated adenosine triphosphatase in ox brain microsomes.化学试剂对牛脑微粒体中与钠钾离子刺激的三磷酸腺苷酶相关的结合磷酸盐周转的影响。
Biochem J. 1970 Nov;120(1):1-13. doi: 10.1042/bj1200001.