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

研究成果: Article査読

4 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)4600-4616
ページ数17
ジャーナルBioorganic and Medicinal Chemistry
16
8
DOI
出版ステータスPublished - 2008 4月 15

ASJC Scopus subject areas

  • 生化学
  • 分子医療
  • 分子生物学
  • 薬科学
  • 創薬
  • 臨床生化学
  • 有機化学

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