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2-(4-Hydroxy-3-nitrophenyl)butanoate

中文名称
——
中文别名
——
英文名称
2-(4-Hydroxy-3-nitrophenyl)butanoate
英文别名
2-(4-hydroxy-3-nitrophenyl)butanoate
2-(4-Hydroxy-3-nitrophenyl)butanoate化学式
CAS
——
化学式
C10H10NO5-
mdl
——
分子量
224.19
InChiKey
PWSAEPCSFKMBBD-UHFFFAOYSA-M
BEILSTEIN
——
EINECS
——
  • 物化性质
  • 计算性质
  • ADMET
  • 安全信息
  • SDS
  • 制备方法与用途
  • 上下游信息
  • 反应信息
  • 文献信息
  • 表征谱图
  • 同类化合物
  • 相关功能分类
  • 相关结构分类

计算性质

  • 辛醇/水分配系数(LogP):
    3
  • 重原子数:
    16
  • 可旋转键数:
    2
  • 环数:
    1.0
  • sp3杂化的碳原子比例:
    0.3
  • 拓扑面积:
    106
  • 氢给体数:
    1
  • 氢受体数:
    5

文献信息

  • ASSAYS FOR DETECTING GLUCOSIDASE ACTIVITY
    申请人:Megazme International Ireland
    公开号:US20150140573A1
    公开(公告)日:2015-05-21
    The present invention relates to a method of detecting α-(1→6)-glucosidase activity in a sample. The method is for example useful for determining the limit dextrinase activity in a sample. The method involves use of an oligosaccharide substrate of the formula X-(glucoside)n-*(glucoside)m-Z—Y, where X is a blocking group, -* is a α-(1→6)-glucosidic linkage and Y is a detectable label. Upon cleavage of the α-(1→6)-glucosidic linkage, the detectable label is released and thus the α-(1→6)-glucosidase activity can be determined. The invention also relates to the oligosaccharide substrate per se.
    本发明涉及一种检测样品中α-(1→6)-葡萄糖苷酶活性的方法。该方法例如可用于确定样品中极限糊精酶活性。该方法涉及使用式子为X-(葡萄糖苷)n-*(葡萄糖苷)m-Z-Y的寡糖基质,其中X是阻断基,-*是α-(1→6)-葡萄糖苷键,Y是可检测标记。在α-(1→6)-葡萄糖苷键的裂解后,可检测标记被释放,从而可以确定α-(1→6)-葡萄糖苷酶活性。本发明还涉及该寡糖基质本身。
  • [EN] ASSAYS FOR DETECTING GLUCOSIDASE ACTIVITY<br/>[FR] ESSAIS POUR LA DÉTECTION D'ACTIVITÉ DE GLUCOSIDASE
    申请人:CARLSBERG AS CARLSBERG FORSKNINGSCT
    公开号:WO2013185771A1
    公开(公告)日:2013-12-19
    The present invention relates to a method of detecting α-(1→6)-glucosidase activity in a sample. The method is for example useful for determining the limit dextrinase activity in a sample. The method involves use of an oligosaccharide substrate of the formula X- (glucoside) n -*(glucoside) m -Z-Y, where X is a blocking group, -* is a α-(1→6)-glucosidic linkage and Y is a detectable label. Upon cleavage of the α-(1→6)-glucosidic linkage, the detectable labelis released and thus the α-(1→6)-glucosidase activity can be determined. The invention also relates to the oligosaccharide substrate per se.
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