Publication: Purification and characterization of α-glucosidase I from Japanese honeybee (Apis cerana japonica) and molecular cloning of Its cDNA
Issued Date
2006-12-01
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13476947
09168451
09168451
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2-s2.0-33845897678
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Mahidol University
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SCOPUS
Bibliographic Citation
Bioscience, Biotechnology and Biochemistry. Vol.70, No.12 (2006), 2889-2898
Suggested Citation
Jintanart Wongchawalit, Takeshi Yamamoto, Hiroyuki Nakai, Young Min Kim, Natsuko Sato, Mamoru Nishimoto, Masayuki Okuyama, Haruhide Mori, Osamu Saji, Chanpen Chanchao, Siriwat Wongsiri, Rudee Surarit, Jisnuson Svasti, Seiya Chiba, Atsuo Kimura Purification and characterization of α-glucosidase I from Japanese honeybee (Apis cerana japonica) and molecular cloning of Its cDNA. Bioscience, Biotechnology and Biochemistry. Vol.70, No.12 (2006), 2889-2898. doi:10.1271/bbb.60302 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/22940
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Title
Purification and characterization of α-glucosidase I from Japanese honeybee (Apis cerana japonica) and molecular cloning of Its cDNA
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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.