Rabbit liver phosphofructokinase: Rapid purification and phosphorylation site identification

Biochemical and Biophysical Research Communications

Volumn 222, Issue 2, 1996, Pages 410-415

  Zhao, Zhizhuang ^a,b   Pascalar, Robert W ^a   Malencik, Dean A ^a   Anderson, Sonia R ^a  

^a OREGON STATE UNIVERSITY   (United States)

^b VANDERBILT UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

6 PHOSPHOFRUCTOKINASE; CYANOGEN BROMIDE; CYCLIC AMP DEPENDENT PROTEIN KINASE; LIVER ENZYME; PROTAMINE SULFATE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; ENZYME PURIFICATION; PRIORITY JOURNAL;

ORYCTOLAGUS CUNICULUS;

EID: 0030585384     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.1996.0758     Document Type: Article

References (25)

1. 1. Pilkis, S. J., El-Maghrabi, M. R., Pilkis, J., and Claus, T. H. (1982) Arch. Biochem. Biophys. 215, 379-389.
2. 2. Sakakibara, R., and Uyeda, K. (1983) J. Biol. Chem. 258, 8656-8662.
3. 3. Foe, L. G., and Kemp, R. G. (1984) Arch. Biochem. Biophys. 228, 503-511.
4. 4. Domenech, C. E., Mieskes, G., and Söling, H. D. (1988) Eur. J. Biochem. 173, 79-84.
5. 5. Pilkis, S. J., Claus, T. H., Kountz, P. D., and El-Maghrabi, M. R. (1987) in The Enzymes (Boyer, P. D. and Krebs, E. G., Eds.) Vol. 17, pp. 3-46, Academic Press, San Diego.
6. 6. Kemp, R. G., Foe, L. G., Latshaw, S. P., Poorman, R. A., and Heinrikson, R. I. (1981) J. Biol. Chem. 256, 7282-7286.
7. 7. Zhao, Z., Malencik, D. A., and Anderson, S. R. (1991) Biochemistry 30, 2204-2216.
8. 8. Valaitis, A P., Foe, L. G., Kwiatkowska, D., Latshaw, S. P., and Kemp, R. G. (1989) Biochim. Biophys. Acta 995, 187-194.
9. 9. Tsai, M. Y., and Kemp, R. G. (1973) J. Biol. Chem. 248, 785-792.
10. 10. Brock, D. J. H. (1969) Biochem. J. 113, 235-242.
11. 11. Ramaiah, A., and Tejwani, G. A. (1970) Biochem. Biophys. Res. Commun. 39, 1149-1156.
12. 12. Kemp, R. G. (1971) J. Biol. Chem. 246, 245-252.
13. 13. Massey, T. H., and Deal, W. C. (1973) J. Biol. Chem. 248, 56-62.
14. 14. Brand, I. A., and Soling, H. D. (1974) J. Biol. Chem. 149, 7824-7831.
15. 15. Reinhart, G. D., and Lardy, H. A. (1980) Biochemistry 19, 1477-1484.
16. 16. Kasten, T. P., Naqui, D., Kruep, D., and Dunaway, G. A. (1983) Biochem. Biophys. Res. Commun. 111, 462-469.
17. 17. Toda, T., and Ohashi, M. (1986) J. Biol. Chem. 261, 12455-12461.
18. 18. Koyama, T., Ema, T., Hashizume, N., Hachimori, A., and Iizuka, E. (1988) Comp. Biochem. Physiol. 93B, 517-521.
19. 19. Peters, K. A., Demaille, J. G., and Fischer, E. H. (1977) Biochemistry 16, 5691-5697.
20. 20. Racker, E. (1947) J. Biol. Chem. 167, 843-854.
21. 21. Bradford, M. M. (1976) Anal. Biochem. 72, 248-254.
22. 22. Welch, P., and Scopes, R. K. (1981) Anal. Biochem. 112, 154-157.
23. 23. Reinhart, G. D., and Lardy, H. A. (1980) Biochemistry 19, 1491-1495.
24. 24. Huang, T.-S., Feramisco, J. R., Glass, D. B., and Krebs, E. G. (1979) In From Gene to Protein: Information Transfer in Normal and Abnormal Cells (T. R. Russell, K. Brew, H. Faber, and J. Schultz, Eds.) pp. 449-461. Academic Press, New York.
25. 25. Gehnrich, S. C., Gekakis, N., and Sul, H. S. (1988) J. Biol. Chem. 263, 11755-11759.