Affinity purification and characterization of a key enzyme responsible for circadian rhythmic control of nyctinasty in Lespedeza cuneata L.
The synthesis of an affinity gel aimed at leaf-opening factor beta-glucosidase (LOFG) and affinity purification of LOFG is presented. A gluconamidine-based beta-glucosidase inhibitor was used as the ligand of the affinity gel. beta-Glucosidase exhibiting an activity shift throughout the day was selectively purified from Lespedeza cuneata Don by the affinity gel. The resulting LOFG exhibited high substrate specificity toward the leaf-opening factor.
Kato
Eisuke
E
Department of Chemistry, Tohoku University, Sendai 980-8578, Japan.
Sasaki
Takehiko
T
Ueda
Minoru
M
D001234:Aspergillus niger / Q000187:drug effects / Q000201:enzymology; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002940:Circadian Rhythm; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005959:Glucosidases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D029884:Lespedeza / Q000201:enzymology*; D008024:Ligands; D008969:Molecular Sequence Data; D015394:Molecular Structure; D018515:Plant Leaves / Q000201:enzymology; D018521:Plant Physiological Phenomena; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D008024:Ligands; D005959:Glucosidases