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Physiological correlation between glycyrrhizin, glycyrrhizin‐binding lipoxygenase and casein kinase II
Author(s) -
Shimoyama Yoshihito,
Ohtaka Hisayuki,
Nagata Nobuyuki,
Munakata Hiroshi,
Hayashi Norio,
Ohtsuki Kenzo
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00744-2
Subject(s) - glycyrrhizin , phosphorylation , chemistry , biochemistry , lipoxygenase , enzyme , kinase , protein kinase a , microbiology and biotechnology , affinity chromatography , biology , pharmacology
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 μM GL, but inhibited by 30 μM GL or 10 μM oGA; and (ii) gbLOX activity is enhanced when the enzyme is phosphorylated by CK‐II in the presence of 3 μM 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.