Purification and characterization of phosphofructokinase from the yeast Kluyveromyces lactis

Yeast

Volumn 13, Issue 14, 1997, Pages 1309-1317

  Bär, Jörg ^a   Schellenberger, Wolfgang ^a   Kopperschläger, Gerhard ^a  

^a UNIVERSITY HOSPITAL LEIPZIG   (Germany)

Author keywords

Kluyveromyces lactis; Molecular and kinetic properties; Phosphofructokinase; Protein purification

Indexed keywords

6 PHOSPHOFRUCTOKINASE; PHOSPHOTRANSFERASE;

AFFINITY CHROMATOGRAPHY; ARTICLE; CONTROLLED STUDY; ENZYME PURIFICATION; GEL ELECTROPHORESIS; GEL PERMEATION CHROMATOGRAPHY; KLUYVEROMYCES; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; YEAST;

EID: 0030838251     PISSN: 0749503X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-0061(199711)13:14<1309::aid-yea181>3.0.co;2-%23     Document Type: Article

References (19)

1. Aguilera, A. and Zimmermann, F. K. (1986). Isolation and molecular analysis of the phosphoglucose isomerase structural gene of Saccharomyces cerevisiae. Mol. Gen. Genet. 202, 83-89.
2. Bradford, M. M. (1976). A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
3. Boles, E., Lehnert, W. and Zimmermann, F.K. (1993). The role of the NAD-dependent glutamate dehydrogenase in restoring growth on glucose of a Saccharomyces cerevisiae phosphoglucose isomerase mutant. Eur. J. Biochem. 217, 469-477.
4. Cohn, E. J. and Edsall, J. T. (1943). Proteins, Amino Acids and Peptides as Ions and Dipolar Ions. Reinhold, New York.
5. Goffrini, P., Wėselowski-Louvel, M. and Ferrero, I. (1991). Phosphoglucose isomerase gene is involved in the Rag phenotype of the yeast Kluyveromyces lactis. Mol. Gen. Genet. 128, 401-409.
6. Gonzáles Siso, M. I., Freire Picos, M. A. and Cerdán, M. E. (1996). Reoxidation of the NADPH produced by the pentose phosphate pathway is necessary for utilization of glucose by Kluyveromyces lactis rag2 mutants. FEBS Lett. 387, 7-10.
7. Heinisch, J., Kirchrath, L., Liesen, T., Vogelsang, K. and Hollenberg, C. P. (1993). Molecular genetics of phosphofructokinase in the yeast Kluyveromyces lactis. Mol. Microbiol. 8, 559-570.
8. Heinisch, J., Boles, E. and Timpel, C. (1996). A yeast phosphofructokinase insensitive to the allosteric activator fructose 2,6-bisphosphate. J. Biol. Chem. 271, 15928-15933.
9. Hofmann, E. and Kopperschläger, G. (1982). Phosphofructokinase from yeast. Methods Enzymol. 90, 49-60.
10. Huse, K. and Kopperschläger, G. (1983). Interactions of antibodies against phosphofructokinase with the soluble and particulate enzymes from yeast. FEBS Lett. 155, 50-54.
11. Kopperschläger, G., Bär, J., Nissler, K. and Hofmann, E. (1977). Physicochemical parameters and subunit composition of yeast phosphofructokinase. Eur. J. Biochem. 81, 317-325.
12. Kopperschläger, G., Bär, J. and Stellwagen, E. (1993). Limited proteolysis of yeast phosphofructokinase. Eur. J. Biochem. 217, 527-533.
13. Kopperschläger, G., Kriegel, Th. and Birkenmeier, G. (1995). Interaction of murine monoclonal subunit-specific antibodies with phosphofructokinase from Saccharomyces cerevisiae. FEBS Lett. 363, 17-21.
14. Laemmli, U. K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685.
15. McRorie, D. K. and Voelker, P. J. (1993). Self-Associating Systems in the Analytical Ultracentrifuge Beckman Instruments Inc., Palo Alto.
16. Monod, J., Wyman, J. and Changeux, J. P. (1965). On the nature of allosteric transitions: A plausible model. J. Mol Biol. 12, 88-118.
17. Nissler, K., Otto, A., Schellenberger, W. and Hofmann, E. (1983). Similarity of activation of yeast phosphofructokinase by AMP and fructose 2,6-bisphosphate. Biochem. Biophys. Res. Commun. 111, 294-300.
18. Schröter, A. and Kopperschläger, G. (1996). 6-Phosphofructo-1-kinase from the lipid-accumulating, non-fermentative, red yeast Rhodotorula glutinis. FEMS Microbiol. Lett. 142, 247-252.
19. Tijane, M. N., Seydoux, F. J., Hill, M., Roucous, C. and Laurent, M. (1979). Octameric structure of yeast phosphofructokinase as determined by crosslinking with disuccinimidyl β-hydromuconate. FEBS Lett. 105, 249-253.