Comparative Abilities and Optimal Conditions for β-Glycosidase Enzymes to Hydrolyse the Glucuronide,Glucoside,and N-Acetylglucosaminide Conjugates of Bile Acids
書誌事項
- タイトル別名
-
- Comparative Abilities and Optimal Conditions for .BETA.-Glycosidase Enzymes to Hydrolyse the Glucuronide, Glucoside, and N-Acetylglucosaminide Conjugates of Bile Acids.
- Comparative Abilities and Optimal Condi
この論文をさがす
抄録
Enzymatic hydrolyses were described for three variants of glycosidic conjugated bile acids with one β-glucuronidase (Helix pomatia), three β-glucosidase (almonds, sweet almonds, and Escherichia coli), and four β-N-acetylglucosaminidase (Jack beans, bovine kidney, human placenta, and Diplococcus pneumoniae) preparations. The substrates include the β-glucuronide, β-glucoside, and β-N-acetylglucosaminide conjugates of bile acids related to hyodeoxycholic, murideoxycholic, chenodeoxycholic, and ursodeoxycholic acids possessing a sugar moiety at position C-3, C-6 or C-7. The comparative abilities and optimal conditions for the β-glycosidases to catalyze the hydrolyses of the substrates were clarified by changing pHs and incubation times. Hydrolysis rates of the bile acid glycosides with β-glycosidase treatments were influenced by both the source of the enzyme preparations and the conjugated position of a sugar moiety in the substrates, and the 3-glucoside and 3-N-acetylglucosaminide conjugates were usually hydrolyzed more efficiently than their corresponding 6- and 7-analogs. Escherichia coli and jack bean enzymes were chosen to hydrolyse the glucosidic and N-acetylglucosaminidic conjugated bile acids, respectively.
収録刊行物
-
- Biological & Pharmaceutical Bulletin
-
Biological & Pharmaceutical Bulletin 20 (8), 828-833, 1997
公益社団法人 日本薬学会
- Tweet
キーワード
詳細情報 詳細情報について
-
- CRID
- 1390282679600139904
-
- NII論文ID
- 110003639157
-
- NII書誌ID
- AA10885497
-
- ISSN
- 13475215
- 09186158
-
- NDL書誌ID
- 4287937
-
- PubMed
- 9300125
-
- 本文言語コード
- en
-
- データソース種別
-
- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
-
- 抄録ライセンスフラグ
- 使用不可