Isolation and characterization of the two active fractions from porcine brain phosphofructokinase purified by affinity chromatography.
Phosphofructokinase was purified from porcine brain by the successive affinity chromatographies of Blue-Sepharose and ATP-agarose. The purified enzyme was found to contain three subunits, namely, the L-, M- and C-type by SDS-polyacrylamide gel electrophoresis (SDS-PAGE). The purified enzyme separated into the two active fractions through gel filtration (FIs and FIIs). SDS-PAGE revealed that the FIs contained the L- and M-type subunits, while the FIIs contained the M- and C-type. The FIIs preparation was more sensitive to ATP inhibition, ADP activation and citrate inhibition than the FIs.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002846:Chromatography, Affinity / Q000379:methods; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D010732:Phosphofructokinase-1 / Q000302:isolation & purification* / Q000378:metabolism; D013552:Swine
D007527:Isoenzymes; D010732:Phosphofructokinase-1