Activation by calcium of AMP deaminase from the human red cell.
We have investigated the effects of Ca2+ on AMP deaminase from human red cells. At variance with the other known modulators, Ca2+ increased the apparent affinity for AMP without modifying the characteristic positive cooperativity of the enzyme towards the substrate. Ca2+ sensitivity was not modified by dialysis, but dilution of the haemolysate produced an activation of the enzyme similar to that induced by Ca2+. Simultaneously, the Ca2+ dependence was lost. The sensitivity to other modulators, such as ATP, diphosphoglycerate or phosphate, was not modified by dilution. Partial purification of the enzyme produced the same effects as haemolysate dilution. These results may be interpreted to mean that Ca2+ acts by antagonizing an endogenous inhibitor present in red cell lysates.
Almaraz
L
L
Departamento de Bioquímica y Biología Molecular y Fisiologia, Facultad de Medicina, Universidad de Valladolid, Spain.
García-Sancho
J
J
D019794:2,3-Diphosphoglycerate; D000659:AMP Deaminase / Q000097:blood*; D000255:Adenosine Triphosphate / Q000494:pharmacology; D002118:Calcium / Q000494:pharmacology*; D004163:Diphosphoglyceric Acids / Q000494:pharmacology; D004789:Enzyme Activation; D004912:Erythrocytes / Q000201:enzymology*; D006461:Hemolysis; D006801:Humans; D007700:Kinetics; D009709:Nucleotide Deaminases / Q000097:blood*
D004163:Diphosphoglyceric Acids; D019794:2,3-Diphosphoglycerate; D000255:Adenosine Triphosphate; D009709:Nucleotide Deaminases; D000659:AMP Deaminase; D002118:Calcium