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Purification and properties of pyruvate kinase from Dictyostelium discoideum
1School of Biological Sciences, Flinders University Bedford Park, S.A., Australia.
Biochemistry International
|January 1, 1990
Abstract:
Pyruvate kinase (EC 2.7.1.40) from aggregating Dictyostelium discoideum cells has been purified to homogeneity. It has a monomeric molecular weight of 66kD and is tetrameric in low ionic strength buffers. The enzyme is not regulated by fructose 1,6-bisphosphate or by alanine and appears to resemble the M1 isoenzyme from rat liver most closely, although its activity is not inhibited by ATP.