The plasma membrane Ca2+ pump mutant lysine591 → arginine retains some activity, but is still inactivated by fluorescein isothiocyanate

Biochemical Journal

Volumn 317, Issue 1, 1996, Pages 41-44

  Adamo, Hugo P ^a   Filoteo, Adelaida G ^b   Penniston, John T ^b  

^a Instituto de Quimica y Fisicoquimica Biologicas Buenos Aires   (Argentina)

^b MAYO CLINIC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE; ARGININE; FLUORESCEIN ISOTHIOCYANATE; LYSINE; CALCIUM ION; MUTANT PROTEIN;

ARTICLE; CELL MEMBRANE; COMPARATIVE STUDY; DRUG ANTAGONISM; DRUG EFFECT; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; MUTATION; NUCLEOTIDE SEQUENCE; PHOSPHORYLATION; SITE DIRECTED MUTAGENESIS; AMINO ACID SUBSTITUTION; ANIMAL CELL; CALCIUM TRANSPORT; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

ADENOSINE TRIPHOSPHATE; ARGININE; BASE SEQUENCE; CALCIUM-TRANSPORTING ATPASES; CELL MEMBRANE; FLUORESCEIN-5-ISOTHIOCYANATE; HUMANS; LYSINE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHOSPHORYLATION;

EID: 0029887537     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3170041     Document Type: Article

References (26)

1. Pedersen, P. L. and Carafoli, E. (1987) Trends Biochem. Sci. 12, 145-150
2. Pedersen, P. L. and Carafoli, E. (1987) Trends Biochem. Sci. 12, 185-189
3. Karlish, S. J. D. (1980) J. Bioenerg. Biomembr. 12, 111-136
4. Pick, U. and Karlish, S. J. D. (1980) Biochim. Biophys. Acta 626, 255-261
5. Muallem, S. and Karlish, S. J. D. (1983) J. Biol. Chem. 258, 169-175
6. Filoteo, A. G., Gorski, J. P. and Penniston, J. T. (1987) J. Biol. Chem. 262, 6526-6530
7. Taylor, W. R. and Green, N. M. (1989) Eur. J. Biochem. 179, 241-248
8. Pick, U. (1981) Eur. J. Biochem. 121, 187-195
9. Ellis-Davies, G. C. R. and Kaplan, J. H. (1993) J. Biol. Chem. 268, 11622-11627
10. Gatto, C. and Milanick, M. A. (1994) in The Sodium Pump (Bamberg and Schoner, eds.), pp. 609-612, Steinkopp, Darmstadt, and Springer, New York
11. Adamo, H. P., Verma, A. K., Sanders, M. A., Heim, R., Salisbury, J. L., Wieben, E. D. and Penniston, J. T. (1992) Biochem. J. 285, 791-797
12. Carafoli, E. (1994) FASEB J. 8, 993-1002
13. Gluzman, Y. (1981) Cell 23, 175-182
14. Enyedi, A., Verma, A. K., Filoteo, A. G. and Penniston, J. T. (1993) J. Biol. Chem. 268, 10621-10626
15. Magocsi, M. and Penniston, J. T. (1991) Biochim. Biophys. Acta 1063, 7-14
16. Sarkadi, B., Enyedi, A., Foldes-Papp, Z. and Gardos, G. (1986) J. Biol. Chem. 261, 9552-9557
17. Bradford, M. M. (1976) Anal. Biochem. 72, 248-254
18. Maruyama, K. and MacLennan, D. H. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 3314-3318
19. Serrano, R. and Portillo, F. (1990) Biochim. Biophys. Acta 1018, 195-199
20. Adamo, H. P., Filoteo, A. G., Enyedi, A. and Penniston, J. T. (1995) J. Biol. Chem. 270, 30111-30114
21. Clarke, D. M., Loo, T. W. and MacLennan, D. H. (1990) J. Biol. Chem. 265, 22223-22227
22. Xu, K. (1989) Biochemistry 28, 5764-5772
23. Fletterick, R. J., Bates, D. J. and Steitz, T. A. (1975) Proc. Natl. Acad. Sci. U.S.A. 72, 38-42
24. Yamagata, K., Daiho, T. and Kanazawa, T. (1993) J. Biol. Chem. 268, 20930-20936
25. Hinz, H. R. and Kirley, T. L. (1990) J. Biol. Chem. 265, 10260-10265
26. Wang, K. and Farley, R. A. (1992) J. Biol. Chem. 267, 3577-3580