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

Wongchawalit, Jintanart; Yamamoto, Takeshi; Nakai, Hiroyuki et al.

Bioscience Biotechnology and Biochemistry, 2006, 70(12), 2889-2898

Permalink : https://hdl.handle.net/2115/17235

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アクセス権
open access
URI
https://hdl.handle.net/2115/17235
タイトル
Purification and Characterization of α-Glucosidase I from Japanese Honeybee (Apis cerana japonica) and Molecular Cloning of Its cDNA
著者
Wongchawalit, Jintanart ; Yamamoto, Takeshi ; Nakai, Hiroyuki ; Kim, Young-Min ; Sato, Natsuko ; Nishimoto, Mamoru ; Okuyama, Masayuki ; Mori, Haruhide ; Saji, Osamu ; Chanchao, Chanpen ; Wongsiri, Siriwat ; Surarits, Rudee ; Svasti, Jisnuson ; Chiba, Seiya ; Kimura, Atsuo
著者名
Wongchawalit, Jintanart
著者名
Yamamoto, Takeshi
著者名
Nakai, Hiroyuki
著者名
Kim, Young-Min
著者名
Sato, Natsuko
著者名
Nishimoto, Mamoru
e-Rad_Researcher
00344490
著者名
Okuyama, Masayuki
著者名
Mori, Haruhide
著者名
Saji, Osamu
著者名
Chanchao, Chanpen
著者名
Wongsiri, Siriwat
著者名
Surarits, Rudee
著者名
Svasti, Jisnuson
著者名
Chiba, Seiya
e-Rad_Researcher
90186312
著者名
Kimura, Atsuo
言語
英語
キーワード
Japanese honeybee α-glucosidase
honeybee isoenzymes
western honeybee α-glucosidase
allosteric enzyme
発行日
2006-12
出版者
Japan Society for Bioscience, Biotechnology, and Agrochemistry
収録物名
Bioscience Biotechnology and Biochemistry
巻(号)
70(12)
ページ
2889-2898
抄録
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.
資源タイプ
学術雑誌論文
出版タイプ
Version of Record
PISSN
0916-8451
EISSN
1347-6947
関連情報
PMID
17151473
URI
http://www.jstage.jst.go.jp/
関連情報 (isIdenticalTo)
出版社版DOI
https://doi.org/10.1271/bbb.60302