抄録
Endo-beta-N-acetylglucosaminidase from Flavobacterium sp. released about 30% of the N-linked sugar chains from the glucose oxidase of Aspergillus niger. To elucidate the role of the carbohydrate moiety, the enzymatic properties of native and carbohydrate-depleted glucose oxidases were compared. It was found that their catalytic activities and thermal and pH stabilities were identical. However, the carbohydrate-depleted glucose oxidase was more rapidly precipitated by the addition of trichloroacetic acid and ammonium sulfate than the native enzyme. These results show that the N-linked sugar chains of the glucose oxidase contributed to the high solubility of the enzyme in water.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 460-464 |
| ページ数 | 5 |
| ジャーナル | Biochemistry and cell biology = Biochimie et biologie cellulaire |
| 巻 | 67 |
| 発行部数 | 8 |
| DOI | |
| 出版物ステータス | 出版済み - 1 1 1989 |
| 外部発表 | Yes |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology
これを引用
Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger. / Takegawa, K.; Fujiwara, K.; Iwahara, S.; Yamamoto, K.; Tochikura, T.
：: Biochemistry and cell biology = Biochimie et biologie cellulaire, 巻 67, 番号 8, 01.01.1989, p. 460-464.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger.
AU - Takegawa, K.
AU - Fujiwara, K.
AU - Iwahara, S.
AU - Yamamoto, K.
AU - Tochikura, T.
PY - 1989/1/1
Y1 - 1989/1/1
N2 - Endo-beta-N-acetylglucosaminidase from Flavobacterium sp. released about 30% of the N-linked sugar chains from the glucose oxidase of Aspergillus niger. To elucidate the role of the carbohydrate moiety, the enzymatic properties of native and carbohydrate-depleted glucose oxidases were compared. It was found that their catalytic activities and thermal and pH stabilities were identical. However, the carbohydrate-depleted glucose oxidase was more rapidly precipitated by the addition of trichloroacetic acid and ammonium sulfate than the native enzyme. These results show that the N-linked sugar chains of the glucose oxidase contributed to the high solubility of the enzyme in water.
AB - Endo-beta-N-acetylglucosaminidase from Flavobacterium sp. released about 30% of the N-linked sugar chains from the glucose oxidase of Aspergillus niger. To elucidate the role of the carbohydrate moiety, the enzymatic properties of native and carbohydrate-depleted glucose oxidases were compared. It was found that their catalytic activities and thermal and pH stabilities were identical. However, the carbohydrate-depleted glucose oxidase was more rapidly precipitated by the addition of trichloroacetic acid and ammonium sulfate than the native enzyme. These results show that the N-linked sugar chains of the glucose oxidase contributed to the high solubility of the enzyme in water.
UR - http://www.scopus.com/inward/record.url?scp=0024707969&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024707969&partnerID=8YFLogxK
U2 - 10.1139/o89-072
DO - 10.1139/o89-072
M3 - Article
C2 - 2511903
AN - SCOPUS:0024707969
VL - 67
SP - 460
EP - 464
JO - Biochemistry and Cell Biology
JF - Biochemistry and Cell Biology
SN - 0829-8211
IS - 8
ER -