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

doi:10.1016/j.tetlet.2007.01.085

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

SCI - Chemistry

Tohoku University

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

2 Citations (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 language	English
Pages (from-to)	2409-2413
Number of pages	5
Journal	Tetrahedron Letters
Volume	48
Issue number	13
DOIs	https://doi.org/10.1016/j.tetlet.2007.01.085
Publication status	Published - 2007 Mar 26

Keywords

β-Glucosidase
Affinity chromatography
Gluconamidine
Nyctinast

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10.1016/j.tetlet.2007.01.085

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title = "Affinity purification of the key enzyme of nyctinasty controlling the rhythm of leaf movement using gluconamidine ligand",

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.",

keywords = "β-Glucosidase, Affinity chromatography, Gluconamidine, Nyctinast",

author = "Eisuke Kato and Takehiko Sasaki and Tadahiro Kumagai 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), and JSPS Grant for E.K.",

year = "2007",

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doi = "10.1016/j.tetlet.2007.01.085",

language = "English",

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T1 - Affinity purification of the key enzyme of nyctinasty controlling the rhythm of leaf movement using gluconamidine ligand

AU - Kato, Eisuke

AU - Sasaki, Takehiko

AU - Kumagai, Tadahiro

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), and JSPS Grant for E.K.

PY - 2007/3/26

Y1 - 2007/3/26

N2 - 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.

AB - 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.

KW - β-Glucosidase

KW - Affinity chromatography

KW - Gluconamidine

KW - Nyctinast

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M3 - Article

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VL - 48

SP - 2409

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JO - Tetrahedron Letters

JF - Tetrahedron Letters

IS - 13

ER -

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

Abstract

Keywords

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