Na,K-ATPase: The role of state of lipids and Mg ions in activity regulation

Abstract

FEBS LettersVolume 80, Issue 2 p. 303-307 Full-length articleFree Access Na,K-ATPase: The role of state of lipids and Mg ions in activity regulation A. Boldyrev, A. Boldyrev Department of Biochemistry and Department of Biophysics, Moscow State University, Moscow 117234, USSRSearch for more papers by this authorE. Ruuge, E. Ruuge Department of Biochemistry and Department of Biophysics, Moscow State University, Moscow 117234, USSRSearch for more papers by this authorI. Smirnova, I. Smirnova Department of Biochemistry and Department of Biophysics, Moscow State University, Moscow 117234, USSRSearch for more papers by this authorM. Tabak, M. Tabak Department of Biochemistry and Department of Biophysics, Moscow State University, Moscow 117234, USSRSearch for more papers by this author A. Boldyrev, A. Boldyrev Department of Biochemistry and Department of Biophysics, Moscow State University, Moscow 117234, USSRSearch for more papers by this authorE. Ruuge, E. Ruuge Department of Biochemistry and Department of Biophysics, Moscow State University, Moscow 117234, USSRSearch for more papers by this authorI. Smirnova, I. Smirnova Department of Biochemistry and Department of Biophysics, Moscow State University, Moscow 117234, USSRSearch for more papers by this authorM. Tabak, M. Tabak Department of Biochemistry and Department of Biophysics, Moscow State University, Moscow 117234, USSRSearch for more papers by this author First published: August 15, 1977 https://doi.org/10.1016/0014-5793(77)80463-8Citations: 12AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat References 1 L. Tsakadze, Z.P. Kometiani, Soobshch. Akad. Nauk Gruz. SSR, 60, (1970), 449– 452. 2 J. Charnock, D.A. Cook, L. Opit, Nature New Biol., 233, (1971), 171– 172. 3 J. Charnock, D. Doty, J.C. Russel, Arch. Biochem. Biophys., 142, (1971), 633– 637. 4 A. Chipperfield, R. Whittam, Proc. Roy. Soc. London, A187, (1974), 269– 280. 5 A.A. Boldyrev, Usp. Biol. Khim., 18, (1977), 122– 139. 6 M. Dixon, E. Webb, 2nd ed Enzymes (1968), Longmans 7 J. Kumamoto, J. Raison, J. Lyons, J. Theor. Biol., 31, (1971), 47– 51. 8 R.N. Priestland, R. Whittam, J. Physiol., 220, (1972), 353– 9 C.M. Grisham, R. Barnett, Biochemistry, 12, (1973), 2635– 2637. 10 R. Barnett, J. Palazotto, Ann. N.Y. Acad. Sci., 242, (1974), 69– 76. 11 H. Kimelberg, D. Papahadjopoulos, J. Biol. Chem., 249, (1974), 1071– 1080. 12 J. Charnock, A. Almeida, R. To, Arch. Biochem. Biophys., 167, (1975), 480– 487. 13 A.A. Boldyrev, 10th Int. Congr. of Biochem. Hamburg, (1976), 06-6-235 14 T. Hexum, F. Samson, R. Himes, Biochim. Biophys. Acta, 212, (1970), 322– 331. 15 A.A. Boldyrev, V.A. Tkachuk, V.P.K. Titanji, Biochim. Biophys. Acta, 357, (1974), 319– 324. 16 I. Klodos, P. Ottolenghi, A. Boldyrev, Analyt. Biochem., 67, (1975), 397– 403. 17 K. Bowler, C. Dunkan, Comp. Biochem. Physiol., 24, (1968), 1043– 1054. 18 H. Kimelberg, Biochim. Biophys. Acta, 413, (1975), 143– 156. 19 W. Fiehn, J.B. Peter, J.F. Mead, M. Gan-Elepafio, J. Biol. Chem., 246, (1971), 5617– 5620. 20 K. Jacobson, D. Papahajopoulos, Biochemistry, 14, (1975), 152– 161. 21 M. Tabak, I. Smirnova, E. Ruuge, V. Tverdislov, Biofizika, 22, (1977), 217– 222. 22 S. Hilden, L. Hokon, J. Biol. Chem., 250, (1975), 6296– 6303. 23 F. Brinley, L.J. Mullins, J. Gen. Physiol., 52, (1968), 181– 211. 24 P.J. Garrahan, A. Rega, J. Physiol., 233, (1972), 595– 617. Citing Literature Volume80, Issue2August 15, 1977Pages 303-307 ReferencesRelatedInformation