Guanosine triphosphatase activity in human erythrocyte membranes.
Human red cell membranes have the capacity to hydrolyze enzymatically GTD to GDP. The reaction requires magnesium, is not appreciably affected by sodium, potassium or calcium, and is not inhibited by ouabain. Kinetic analysis suggests that there are two separate enzymes in membranes which cleave GTP, a 'high Km' GTPase and a 'low Km' GTPase. Both enzymes are also ATPases, with an approximately equal affinity for GTP and ATP. GTPase activity did not extract from the membrane with spectrin and was not inactivated by antispectrin antibody. Activity was partially destroyed by 0.5% Triton X-100. It seems probable that the low Km GTPase is the sodium- and potassium-independent ATPase of red cell membranes. The identity of the high Km enzyme is not clear.
D000251:Adenosine Triphosphatases / Q000097:blood; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D020558:GTP Phosphohydrolases / Q000097:blood*; D006801:Humans; D007700:Kinetics; D008670:Metals / Q000494:pharmacology; D009711:Nucleotides / Q000494:pharmacology; D010042:Ouabain / Q000494:pharmacology; D010744:Phosphoric Monoester Hydrolases / Q000097:blood*
D008670:Metals; D009711:Nucleotides; D010042:Ouabain; D010744:Phosphoric Monoester Hydrolases; D000251:Adenosine Triphosphatases; D020558:GTP Phosphohydrolases