Affinity purification and characterization of a key enzyme responsible for circadian rhythmic control of nyctinasty in Lespedeza cuneata L

Eisuke Kato, Takehiko Sasaki, Minoru Ueda

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

The synthesis of an affinity gel aimed at leaf-opening factor β-glucosidase (LOFG) and affinity purification of LOFG is presented. A gluconamidine-based β-glucosidase inhibitor was used as the ligand of the affinity gel. β-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.

Original languageEnglish
Pages (from-to)4600-4616
Number of pages17
JournalBioorganic and Medicinal Chemistry
Volume16
Issue number8
DOIs
Publication statusPublished - 2008 Apr 15

Keywords

  • Affinity purification
  • Gluconamidine
  • Inhibitor
  • Nyctinasty
  • β-Glucosidase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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