ATP-ADP exchange reaction catalyzed by Na+,K+-ATpase: Dephosphorylation by ADP of the E1P enzyme form

Biochemistry

Volumn 36, Issue 46, 1997, Pages 14228-14237

  Campos, Marta ^a   Beaugé, Luis ^a  

^a INSTITUTO DE INVESTIGACIÓN MÉDICA MERCEDES Y MARTÍN FERREYRA   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE;

ANIMAL TISSUE; ARTICLE; CATALYSIS; CONTROLLED STUDY; DEPHOSPHORYLATION; ENZYME ACTIVITY; KIDNEY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; REACTION ANALYSIS; SWINE;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ANIMALS; CATIONS, DIVALENT; CHYMOTRYPSIN; KIDNEY; KINETICS; MAGNESIUM; NA(+)-K(+)-EXCHANGING ATPASE; PEPTIDE FRAGMENTS; PHOSPHATES; SWINE;

EID: 0030671442     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971087c     Document Type: Article

References (39)

1. Glynn, I. M. (1993) J. Physiol. 462, 1-30.
2. Beaugé, L., and Glynn, I. M. (1979) J. Physiol. 289, 17-31.
3. Taniguchi, K., and Post, R. L. (1975) J. Biol. Chem. 250, 3010-3018.
4. Campos, M., and Beáuge, L. (1988) Biochim. Biophys. Acta 944, 242-248.
5. Klodos, I., and Norby, J. G. (1987) Biochim. Biophys. Acta 897, 302-314.
6. Post, R. L., Hegivary, C., and Kume, S. (1977) J. Biol. Chem. 247, 6530-6540.
7. Karlish, S. J. D., and Yates, D. W. (1978) Biochim. Biophys. Acta 527, 115-130.
8. Jorgensen, P., and Petersen, J. (1985) Biochim. Biophys. Acta 821, 319-333.
9. Campos, M., and Beaugé, L. (1992) Biochim. Biophys. Acta 1105, 51-60.
10. Jorgensen, P. (1974) Biochim. Biophys. Acta 256, 36-52.
11. Beaugé, L., and Campos, M. (1983) Biochim. Biophys. Acta 729, 137-149.
12. Glynn, I. M., and Chappell, J. B. (1964) Biochem. J. 90, 147-149.
13. de Meis, L. (1974) Biochemistry 11, 2460-2465.
14. Beaugé, L., and Campos, M. (1986) J. Physiol. 375, 1-25.
15. Lowry, H., Rosebrough, N., Farr, A., and Randall, R. J. (1951) J. Biol. Chem. 93, 265-275.
16. Lichtner, R., and Wolf, H. (1979) Biochem. J. 181, 759-761.
17. Zetteiqvist, O., Mardh, S., and Sandstrom, N. (1976) Anal. Biochem. 71, 544-549.
18. Berger, R. L. (1978) Biophys. J. 24, 2-20.
19. Mercer, R. W., and Dunham, P. B. (1981) J. Gen. Physiol. 66, 375-400.
20. Froehlich, J., Albers, R. W., Koval, G. J., Goebel, R., and Berman, M. (1976) J. Biol. Chem. 251, 2186-2188
21. Forbush, B. (1987) J. Biol. Chem. 262, 11104-11115.
22. Huang, W., Ganjeizadeh, M., Wang, Y., Chiu, I., and Askari, A. (1990) Biochim. Biophys. Acta 1030, 65-72.
23. Glynn, I., Hara, Y., and Richards, D. (1984) J. Physiol. 351, 531-547.
24. Pickart, C. M., and Jencks, W. P. (1982) J. Biol. Chem. 257, 5319-5322.
25. Hobbs, A., Albers, R. W., and Froehlich, J. (1983) Curr. Top. Membr. Transp. 19, 569-572.
26. Hammes, G. G., and Schimmel, P. R. (1970) in The Enzymes (Boyer, P. D., Ed.) pp 67-114, Academic Press, New York.
27. Skou, J. C. (1974) Ann. N.Y. Acad. Sci. 242, 168-184.
28. Glynn, I. M. (1982) Ann. N.Y. Acad. Sci. 402, 287-288.
29. Shani, M., Goldschleger, R., and Karlish, S. J. D. (1987) Biochim. Biophys. Acta 904, 13-21.
30. Esmann, M., and Skou, J. C. (1985) Biochem. Biophys. Res. Commun. 127, 857-863.
31. Post, R. L., Toda, G., and Rogers, F. N. (1975) J. Biol. Chem. 250, 691-701.
32. Campos, M., and Beaugé, L. (1994) J. Biol. Chem. 269, 18028-18036.
33. Beaugé, L., Berberián, G., Campos, M. and Pedemonte, C. (1985) in The Sodium Pump (Glynn, I. M., Ellory, C., Eds.) pp 321-333, The Company of Biologists, Cambridge, U.K.
34. Mardh, S., and Post, R. L. (1977) J. Biol. Chem. 252, 633-638.
35. Albers, R. W. (1967) Annu. Rev. Biochem. 36, 727-756.
36. Klodos, I., and Skou, J. C. (1975) Biochim. Biophys. Acta 391, 474-485.
37. Froehlich, J. P., and Heller, P. F. (1985) Biochemistry 24, 126-136.
38. Hobbs, A., Albers, W., Froehlich, J., and Heller, P. (1985) J. Biol. Chem 260, 2035-2037.
39. Sumida, M., Wang, T., Schwartz, A., Younkin, C., and Froelich, J. P. (1980) J. Biol. Chem. 255, 1497-1503.