Affinity purification of the key enzyme of nyctinasty controlling the rhythm of leaf movement using gluconamidine ligand

Eisuke Kato, Takehiko Sasaki, Tadahiro Kumagai, Minoru Ueda

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Synthesis of affinity gel aimed for leaf-opening factor β-glucosidase (LOFG) and affinity purification of LOFG are presented. Gluconamidine-based β-glucosidase inhibitor was utilized for the ligand of the affinity gel. β-Glucosidase exhibiting activity shift throughout the day was selectively purified from Lespedeza cuneata Don by the affinity gel. The resulting LOFG exhibited a high substrate specificity toward the leaf-opening factor.

Original languageEnglish
Pages (from-to)2409-2413
Number of pages5
JournalTetrahedron Letters
Volume48
Issue number13
DOIs
Publication statusPublished - 2007 Mar 26

Keywords

  • Affinity chromatography
  • Gluconamidine
  • Nyctinast
  • β-Glucosidase

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

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