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J. Biochem, 1976, Vol. 80, No. 2 299-308
© 1976 Japanese Biochemical Society

research-article

Regulation of AMP Deaminase from Chicken Erythrocytes: A Kinetic Study of the Allosteric Interactions

Masataka YOSHINO*, Yasuhiko KAWAMURA** and Nobuaki OGASAWARA***

* Department of Biochemistry, School of Medicine, Yokohama City University Minami-ku, Yokohama, Kanagawa 232
** Department of Biochemistry, School of Medicine, Nagoya University Showa-ku, Nagoya, Aichi 466
*** Department of Biochemistry, Institute for Developmental Research Aichi Prefecture Colony, Kasugai, Aichi 486

The allosteric properties of AMP deaminase [EC 3.5.4.6 [EC] ] from chicken erythrocytes have been qualitatively and quantitatively accounted for by the concerted transition theory of Monod et al., on the assumption that this enzyme has different numbers of binding sites for each ligand. Theoretical curves yield a satisfactory fit for all experimental saturation functions with respect to activation by alkali metals and inhibition by P1, assuming that the numbers of binding sites for AMP, alkali metals, and P1 are 4, 2, and 4, respectively. The enzyme was inhibited by concentrations of ATP and GTP below 0.1 and 0.25 mM, respectively, whereas activation of the enzyme was observed at ATP and GTP concentrations above 0.4 and 1.5 mM, respectively. These unusual kinetics with respect to ATP and GTP could be also accounted for by assuming 2 inhibitory and 4 activating sites for each ligand.


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