Purification and Properties of an Acid .ALPHA.-Glucosidase from Acidobacterium capsulatum.
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- Kishimoto Noriaki
- Department of Food and Lifestyle, Faculty of Food Culture, Kurashiki Sakuyo University
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- Shiraishi Takehiko
- Division of Biological Function and Genetic Resources Science, Faculty of Agriculture, Okayama University
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- Inagaki Kenji
- Division of Biological Function and Genetic Resources Science, Faculty of Agriculture, Okayama University
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- Sugio Tsuyoshi
- Division of Biological Function and Genetic Resources Science, Faculty of Agriculture, Okayama University
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- Tanaka Hidehiko
- Division of Biological Function and Genetic Resources Science, Faculty of Agriculture, Okayama University
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- Tano Tatsuo
- Division of Biological Function and Genetic Resources Science, Faculty of Agriculture, Okayama University
Bibliographic Information
- Other Title
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- Acido bacte riurn capsulaturn由来の酸性α-グルコシダーゼの精製と諸性質
- Purification and Properties of an Acid α-Glucosidase from Acidobacterium capsulatum
- Purification and Properties of an Acid アルファーGlucosidase from Acidobacterium capsulatum
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Description
Acidobacterium capsulatum, an acidophilic, mesophilic and chemoorganotrophic bacterium, constitutively produced the acid α-glucosidase. The enzyme, which was successively purified to homogeneity by CM-Sepharose, Sephacryl S-300 and Mono-S ion-exchange chromatography, was a monomeric protein, whose molecular weight was estimated to be 65, 000 by gel filtration and sodium dodecylsulfate-polyacrylamide gel electrophoresis. The enzyme exhibited optimum.activity at pH 4.5 and 30°C, being stable in the pH 3.5 to 7.0 region and in the range of 10 to 50°C. No activity was detected above pH 7.5 or above 60°C. Its isoelectric point was 7.0. The enzyme hydrolyzed pnitrophenyla-glycoside, oligosaccharides containing α-1, 3 (nigerose), α-1, 4 (maltose), α-1, 6 (isomaltose), and α-1, β-2 linkages (sucrose), and soluble starch and produced α-configurational glucose. These findings indicate that the A. capsulatum enzyme represents a novel type of α-glucosidase exhibiting a broad substrate specificity. Amino terminal analysis by a protein sequencer provided the sequence of the first eighteen residues as Ser-Ala-Thr-Gly-Ala-Pro-Trp-Trp-Lys-Asn-Ala-Val-Ile-Tyr-Glu-Val-Tyr-Pro.
Journal
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 46 (2), 121-127, 1999
The Japanese Society of Applied Glycoscience
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Details 詳細情報について
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- CRID
- 1390282681268959744
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- NII Article ID
- 10008258802
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- NII Book ID
- AN10453916
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- ISSN
- 13403494
- 18807291
- 13447882
- http://id.crossref.org/issn/13447882
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- COI
- 1:CAS:528:DyaK1MXksVOgu78%3D
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- NDL BIB ID
- 4785693
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- Text Lang
- en
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- Data Source
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- JaLC
- IRDB
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed