Open AccessAre the Aerobic and Anaerobic Phosphofructokinases of Escherichia coli Different?
Author(s) -
BABUL Jorge,
ROBINSON John P.,
FRAENKEL Dan G.
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11421.x
Subject(s) - escherichia coli , phosphofructokinase , anaerobic exercise , biochemistry , chemostat , enzyme , fructose , chemistry , polyacrylamide gel electrophoresis , aldolase a , biology , microbiology and biotechnology , chromatography , bacteria , glycolysis , physiology , genetics , gene
Phosphofructokinase has been purified from Escherichia coli strain K‐12 grown in a glucose‐limited chemostat, both aerobically and anaerobically. The enzymes migrated together in polyacrylamide gel electrophoresis, had the same subunit size in denaturing (dodecylsulfate) gels ( M r approx. 34000) and the same kinetic characteristics as described earlier for E. coli phosphofructokinase [ e.g. Blangy et al. (1968) J. Mol. Biol. 31 , 13–35]: a sigmoid curve of velocity vs. fructose 6‐phosphate concentration, activation by ADP, and inhibition by phospho enol pyruvate. Findings [ e.g. Doelle (1975) Eur. J. Biochem. 50 , 335–342] of quite different enzymes in aerobic and anaerobic cells were not confirmed.