The binding of glycolytic enzymes to the cytoskeleton--influence of pH.
In a continuing study of the interactions between glycolytic enzymes and cytoskeletal structure, the influence of a variation of the pH of the eluting medium has been investigated. This treatment resulted in an increased degree of binding of most of the glycolytic enzymes with a decrease in pH, with the most marked increases in binding occurring with phosphofructokinase, glyceraldehydephosphate dehydrogenase, enolase and pyruvate kinase. The significance of this data has been discussed with reference to the relative affinities of interaction of the individual glycolytic components and the physiological correlations of these phenomena.
Shearwin
K
K
Division of Science and Technology, Griffith University, Nathan, Brisbane, Australia.
Masters
C
C
D000818:Animals; D001731:Bisphosphoglycerate Mutase / Q000378:metabolism; D002460:Cell Line; D003599:Cytoskeleton / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D005956:Glucose-6-Phosphate Isomerase / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006168:Guinea Pigs; D006863:Hydrogen-Ion Concentration; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D010751:Phosphopyruvate Hydratase / Q000378:metabolism*; D011770:Pyruvate Kinase / Q000378:metabolism*; D014305:Triose-Phosphate Isomerase / Q000378:metabolism
D007770:L-Lactate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D010732:Phosphofructokinase-1; D011770:Pyruvate Kinase; D005634:Fructose-Bisphosphate Aldolase; D010751:Phosphopyruvate Hydratase; D014305:Triose-Phosphate Isomerase; D005956:Glucose-6-Phosphate Isomerase; D001731:Bisphosphoglycerate Mutase