The effect of metabolic inhibitors on the loss of isocitrate lyase activity from Chlorella
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Isocitrate lyase disappeared from acetate-adapted cells of Chlorella when cells were incubated in darkness with glucose. Loss of activity was particularly rapid in nitrogen-free medium and was accompanied by disappearance of the enzyme protein.
Loss of isocitrate lyase activity was prevented by addition of 2-deoxyglucose, glucosamine, cycloheximide or chloramphenicol.
The rate of loss of activity was increased by addition of 2:4-dinitrophenol but this substance prevented the loss of enzyme protein i.e it protected the inactivated enzyme from degradation.
In vitro studies on the digestion of isocitrate lyase protein by papain showed that the enzyme protein was protected from digestion by its substrate, isocitrate, but that inhibitors of the enzyme, namely phosphoenol pyruvate, succinate, oxaloacetate and pyruvate, provided no protection.
KeywordsGlucose Enzyme Pyruvate Succinate Chloramphenicol
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