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      Physiological correlation between glycyrrhizin, glycyrrhizin-binding lipoxygenase and casein kinase II.

      Febs Letters
      Amino Acid Sequence, Animals, Blotting, Western, Carrier Proteins, metabolism, Casein Kinase II, Chromatography, Affinity, Chromatography, High Pressure Liquid, Glycyrrhetinic Acid, analogs & derivatives, Glycyrrhizic Acid, HSP90 Heat-Shock Proteins, Lipoxygenase, Mice, Molecular Sequence Data, Phosphorylation, Protein-Serine-Threonine Kinases, Soybean Proteins

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          Abstract

          By means of glycyrrhizin (GL)-affinity column chromatography, a GL-binding lipoxygenase (gbLOX) was selectively purified from the partially purified soybean LOX-1 fraction. Polypeptide analysis of the purified gbLOX by SDS-PAGE detected two distinct polypeptides (p96 and p94), which were identical to LOX-3 as determined by their partial N-terminal amino acid sequences. Moreover, it was found that (i) phosphorylation of gpLOX by casein kinase II (CK-II) is significantly stimulated by 3 microM GL, but inhibited by 30 microM GL or 10 microM oGA; and (ii) gbLOX activity is enhanced when the enzyme is phosphorylated by CK-II in the presence of 3 microM GL. These results suggest that (i) CK-II is a kinase responsible for the activation of gbLOX through its specific phosphorylation; and (ii) GL is one of the regulatory substances for specific phosphorylation of gbLOX (LOX-3) by CK-II in plant cells.

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