Add time:09/06/2019         Source:sciencedirect.com

1.1.AMP deaminase (AMP aminohydrolase, EC 3.5.4.6) activities of dialyzed and undialyzed hemolyzates of human erythrocytes in the presence of optimal concentrations of K+ were measured. Whereas the activity of the dialyzed hemolyzate was a linear function of the hemolyzate concentration, that of the undialyzed hemolyzate was not. These results suggested the presence of a dialyzable inhibitor of the enzyme in the hemolyzate.2.2.Effects of several organic phosphates of erythrocytes on AMP deaminase were studied, 2,3-Diphosphoglyceric acid, at concentrations usually found in erythrocytes, was found to be an inhibitor of the enzyme.3.3.The substrate-velocity curve of AMP deaminase is a sigmoid. In the presence of 2,3-diphosphoglyceric acid the curve became more sigmoidal in shape. The effects of varying concentrations of 2,3 diphosphoglyceric acid on AMP deaminase in the presence and absence of ATP were also determined. In the presence of ATP, when the per cent inhibition of velocity was plotted against the concentration of 2,3-diphosphoglyceric acid a sigmoidal curve was obtained.4.4.The data suggest that 2,3-diphosphoglyceric acid may control the adenine nucleotide content of the intact erythrocyte through an allosteric regulation of the AMP deaminase activity.

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