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

doi:10.1016/j.bmc.2008.02.035

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

SCI - Chemistry

Research output: Contribution to journal › Article › peer-review

4 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 language	English
Pages (from-to)	4600-4616
Number of pages	17
Journal	Bioorganic and Medicinal Chemistry
Volume	16
Issue number	8
DOIs	https://doi.org/10.1016/j.bmc.2008.02.035
Publication status	Published - 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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10.1016/j.bmc.2008.02.035

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

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.",

keywords = "Affinity purification, Gluconamidine, Inhibitor, Nyctinasty, β-Glucosidase",

author = "Eisuke Kato and Takehiko Sasaki and Minoru Ueda",

note = "Funding Information: This work was supported by a Grant-in-Aid for Scientific Research on Priority Area 16073216 from the Ministry of Education, Science, Sports, and Culture (MEXT), Asahi Glass Foundation, and Naito Foundation. We thank Assoc. Prof. Jun Hiratake and Prof. Kanzo Sakata (Institute for Chemical Research, Kyoto University) for the helpful discussions and suggestions on this work.",

year = "2008",

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day = "15",

doi = "10.1016/j.bmc.2008.02.035",

language = "English",

volume = "16",

pages = "4600--4616",

journal = "Bioorganic and Medicinal Chemistry",

issn = "0968-0896",

publisher = "Elsevier Limited",

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TY - JOUR

T1 - Affinity purification and characterization of a key enzyme responsible for circadian rhythmic control of nyctinasty in Lespedeza cuneata L

AU - Kato, Eisuke

AU - Sasaki, Takehiko

AU - Ueda, Minoru

N1 - Funding Information: This work was supported by a Grant-in-Aid for Scientific Research on Priority Area 16073216 from the Ministry of Education, Science, Sports, and Culture (MEXT), Asahi Glass Foundation, and Naito Foundation. We thank Assoc. Prof. Jun Hiratake and Prof. Kanzo Sakata (Institute for Chemical Research, Kyoto University) for the helpful discussions and suggestions on this work.

PY - 2008/4/15

Y1 - 2008/4/15

N2 - 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.

AB - 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.

KW - Affinity purification

KW - Gluconamidine

KW - Inhibitor

KW - Nyctinasty

KW - β-Glucosidase

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U2 - 10.1016/j.bmc.2008.02.035

DO - 10.1016/j.bmc.2008.02.035

M3 - Article

C2 - 18308573

AN - SCOPUS:42149107088

SN - 0968-0896

VL - 16

SP - 4600

EP - 4616

JO - Bioorganic and Medicinal Chemistry

JF - Bioorganic and Medicinal Chemistry

IS - 8

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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