Mechanism of aldolase binding to erythrocyte membrane: Part I. Effect of membrane phosphorylation on aldolase association.
The effect of phosphorylation of bovine erythrocyte membrane on association of Fructose 1,6-diphosphate (FDP) aldolase has been investigated. The phosphorylation of the membrane seemed to favour the increased association of the enzyme. With the native and NaCl-depleted membrane, it was observed that the extent of phosphorylation could be correlated with the enzyme association. The experiments with the intact erythrocytes isolated from bovine and rabbit blood employing similar conditions, confirmed these findings. The observations with the membrane and whole cells have been substantiated using [gamma-32P]ATP and [32P] inorganic phosphate. The treatment of the enzyme favouring phosphorylation, did not show association of the enzyme with the membrane. The chemical modification of the membrane, influencing the association of the enzyme could be a possible mechanism for fine regulatory control of the activity.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002417:Cattle; D000242:Cyclic AMP / Q000097:blood; D004910:Erythrocyte Membrane / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000097:blood*; D066298:In Vitro Techniques; D010710:Phosphates / Q000378:metabolism; D010766:Phosphorylation; D051381:Rats; D013045:Species Specificity
D010710:Phosphates; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D005634:Fructose-Bisphosphate Aldolase