Evidence for an interaction between cytosolic aldolase and the ATP-and pyrophosphate-dependent phosphofructokinases in carrot storage roots.
Immunoaffinity chromatography was employed to identify potential plant cytosolic aldolase (ALDc) binding proteins. A clarified homogenate of carrot storage root was chromatographed on a column of protein-A-Sepharose that had been covalently coupled to anti-(carrot root ALDc) immunoglobulin G. The column was washed with phosphate-buffered saline (PBS), followed by step-wise elution with increasing concentrations of NaCl in PBS. Several proteins were eluted following application of the salt gradient. Western blotting identified the major eluting proteins to be the PPi-dependent phosphofructokinase (PFP) and the cytosolic form of the ATP-dependent phosphofructokinase (PFKc), enzymes that are metabolically sequential to ALDc. The results suggest that ALDc may specifically interact with PFP and PFKc in carrots.
Moorhead
G B
GB
Department of Biology, Queen's University, Kingston, Ont., Canada.
Plaxton
W C
WC
D000255:Adenosine Triphosphate / Q000378:metabolism; D002846:Chromatography, Affinity; D003600:Cytosol / Q000201:enzymology; D011756:Diphosphates / Q000378:metabolism; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D005635:Fructosediphosphates / Q000378:metabolism; D006019:Glycolysis; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D011485:Protein Binding; D014675:Vegetables / Q000201:enzymology*
D011756:Diphosphates; D005635:Fructosediphosphates; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1; D005634:Fructose-Bisphosphate Aldolase