| 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)
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