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Purification and Characterization of α-Glucosidase I from Japanese Honeybee (Apis cerana japonica) and Molecular Cloning of Its cDNA

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/17235

Title: Purification and Characterization of α-Glucosidase I from Japanese Honeybee (Apis cerana japonica) and Molecular Cloning of Its cDNA
Authors: Wongchawalit, Jintanart Browse this author
Yamamoto, Takeshi Browse this author
Nakai, Hiroyuki Browse this author
Kim, Young-Min Browse this author
Sato, Natsuko Browse this author
Nishimoto, Mamoru Browse this author
Okuyama, Masayuki Browse this author →KAKEN DB
Mori, Haruhide Browse this author
Saji, Osamu Browse this author
Chanchao, Chanpen Browse this author
Wongsiri, Siriwat Browse this author
Surarits, Rudee Browse this author
Svasti, Jisnuson Browse this author
Chiba, Seiya Browse this author
Kimura, Atsuo Browse this author →KAKEN DB
Keywords: Japanese honeybee α-glucosidase
honeybee isoenzymes
western honeybee α-glucosidase
allosteric enzyme
Issue Date: Dec-2006
Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Journal Title: Bioscience Biotechnology and Biochemistry
Volume: 70
Issue: 12
Start Page: 2889
End Page: 2898
Publisher DOI: 10.1271/bbb.60302
PMID: 17151473
Abstract: α-Glucosidase (JHGase I) was purified from a Japanese subspecies of eastern honeybee (Apis cerana japonica) as an electrophoretically homogeneous protein. Enzyme activity of the crude extract was mainly separated into two fractions (component I and II) by salting-out chromatography. JHGase I was isolated from component I by further purification procedure using CM-Toyopearl 650M and Sephacryl S-100. JHGase I was a monomeric glycoprotein (containing 15% carbohydrate), of which the molecular weight was 82,000. Enzyme displayed the highest activity at pH 5.0, and was stable up to 40 °C and in a pH-range of 4.5–10.5. JHGase I showed unusual kinetic features: the negative cooperative behavior on the intrinsic reaction on cleavage of sucrose, maltose, and p-nitrophenyl α-glucoside, and the positive cooperative behavior on turanose. We isolated cDNA (1,930 bp) of JHGase I, of which the deduced amino-acid sequence (577 residues) confirmed that JHGase I was a member of α-amylase family enzymes. Western honeybees (Apis mellifera) had three α-glucosidase isoenzymes (WHGase I, II, and III), in which JHGase I was considered to correspond to WHGase I.
Relation: http://www.jstage.jst.go.jp/
Type: article
URI: http://hdl.handle.net/2115/17235
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 木村 淳夫

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