The influence of deoxyribonuclease I and cytochalasin D on the release of glycolytic enzymes from digitonized cells.
In permeabilized cells, deoxyribonuclease I has been demonstrated to cause a decrease in the extent of binding to cellular structure of all of the glycolytic enzymes other than phosphofructokinase, with this decrease being most marked for aldolase and glyceraldehydephosphate dehydrogenase. Cytochalasin D, in contrast, did not produce this type of effect. These results have been discussed in relation to the evidence for the existence of a complex of glycolytic enzymes which binds to elements of the cytoplasmic matrix, and the possible organization of this complex.
Chen
N H
NH
School of Science, Griffith University, Nathan, Brisbane, Australia.
Don
M
M
Masters
C
C
D000818:Animals; D002478:Cells, Cultured; D015638:Cytochalasin D; D003572:Cytochalasins / Q000494:pharmacology*; D003593:Cytoplasm / Q000201:enzymology; D003850:Deoxyribonuclease I / Q000494:pharmacology*; D004072:Digitonin / Q000494:pharmacology*; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism; D006019:Glycolysis; D007668:Kidney / Q000201:enzymology; D011485:Protein Binding; D013552:Swine; D013997:Time Factors
D003572:Cytochalasins; D015638:Cytochalasin D; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D003850:Deoxyribonuclease I; D005634:Fructose-Bisphosphate Aldolase; D004072:Digitonin