Evidence for an interaction between cytosolic aldolase and the ATP‐ and pyrophosphate‐dependent phosphofructokinases in carrot storage roots

FEBS Letters

Plaxton, William C.¹  Moorhead, Greg B.G.¹ 

[1] Departments of Biology and Biochemistry, Queen's University, Kingston, Ont., K7L 3N6, Canada

关键词: Enzyme—enzyme interaction;    Glycolysis;    Aldolase;    PPi:d-fructose-6-phosphate 1-phosphotransferase;    ATP:d-fructose-6-phosphate 1-phosphotransferase;    ALDc;    cytosolic fructose-1;    6-bisphosphate aldolase;    PFP;    PPi-dependent phosphofructokinase;    PFKc;    cytosolic ATP-dependent phosphofructokinase;    PKc;    cytosolic pyruvate kinase;    GAPDH;    glyceraldehyde-3-phosphate dehydrogenase;    GDH;    glycerol-3-phosphate dehydrogenase;    FBPase;    fructose-1;    6-bisphosphatase.;   

DOI  :  10.1016/0014-5793(92)81208-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Immunoaffinity chromatography was employed to identify potential plant cytosolic aldolase (ALD_c) 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 ALD,) 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 PP_i-dependent phosphofructokinase (PFP) and the cytosolic form of the ATP-dependent phosphofructokinase (PFK_c), enzymes that are metabolically sequential to ALD_c. The results suggest that ALD_c may specifically interact with PFP and PFK_c in carrots.

【 授权许可】

Unknown