Abstract
Ornithine decarboxylase (ODC) forms a stable complex with its antizyme (Az), a non-competitive protein inhibitor of ODC. The complex formation of ODC with Az occurs very rapidly and is dissociated by high salt concentrations e.g., 10% ammonium sulfate. When ODC and Az were mixed in the presence of increasing concentrations of Mg2+, a relief of ODC inhibition by Az was obtained. Complete relief of inhibition occurred at 2.0 mM of MgCl2. Other bivalent cations Ca2+, Ba2+, Co2+, Mn2+, Zn2+ as well as the monocations Na+ and K+ caused similar effect. The polyamines putrescine, spermidine and spermine also caused relief of the in vitro inhibition of ODC by Az. Therefore, the in vivo inactivation of ODC by forming the ODC-Az complex is dependent on the intracellular amounts of salt and polyamines.
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Koromilas, A.E., Kyriakidis, D.A. Reversal of antizyme-induced inhibition of ornithine decarboxylase by cations in barley seedlings. Plant Growth Regul 6, 267–275 (1987). https://doi.org/10.1007/BF00024507
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DOI: https://doi.org/10.1007/BF00024507