β-Gal-(1->3)-α-Gal-OC6H4NO2-p | 86021-56-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: β-Gal-(1->3)-α-Gal-OC6H4NO2-p
• 英文别名: p-nitrophenyl 3-O-β-galactopyranosyl-α-D-galactopyranoside；p-nitrophenyl 3-O-beta-galactopyranosyl-alpha-D-galactopyranoside；(2S,3R,4S,5R,6R)-2-[(2R,3S,4S,5R,6R)-3,5-dihydroxy-2-(hydroxymethyl)-6-(4-nitrophenoxy)oxan-4-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol
• CAS: 86021-56-9
• 化学式: C₁₈H₂₅NO₁₃
• 分子量: 463.395
• InChiKey: LBTDRWMZFQVCAR-PRHRXBDDSA-N

物化性质

• 沸点：
  814.5±65.0 °C(Predicted)
• 密度：
  1.70±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -2
• 重原子数：
  32
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  224
• 氢给体数：
  7
• 氢受体数：
  13

反应信息

• 作为反应物：
  描述：

  β-Gal-(1->3)-α-Gal-OC6H4NO2-p 在 palladium-carbon 作用下， 以 甲醇 为溶剂， 生成 p-aminophenyl 3-O-β-D-galactopyranosyl-α-D-galactopyranoside
  参考文献：
  名称：

  Conjugates comprising galactose &agr;1,3 galactosyl epitopes and methods of using same

  摘要：

  这项发明提供了用于异种移植的共轭物，包括将半乳糖α1,3半乳糖基（αGal）表位共轭到一个价位平台分子上，最好是化学定义的价位平台分子，可以实现精确的价位。该发明还提供了包含这些共轭物的组合物，以及使用这些共轭物和组合物的方法（例如诱导耐受的方法）。

  公开号：

  US06399578B1
• 作为产物：
  描述：

  尾-D-Galactoside,2-nitrophenyl(9CI) 、 4-硝基苯基-α-D-吡喃半乳糖苷 在 β-D-galactosidase from B. circulans ATCC 313 、 sodium acetate 作用下， 以 水 为溶剂， 反应 12.0h， 以9.3%的产率得到β-Gal-(1->3)-α-Gal-OC6H4NO2-p
  参考文献：
  名称：

  通过用β-D-半乳糖苷酶的转糖基作用区域选择性合成β-D-半乳糖吡喃糖基-二糖的对硝基苯基糖苷。

  摘要：

  来自猪肝的β-D-半乳糖苷酶分别诱导Gal，GlcNAc和GalNAc的对硝基苯基糖苷受体从β-D-Gal-OC6H4NO2-o到β-6-D-Gal-OC6H4NO2-o的区域特异性转糖基化，从而提供β -Gal-（1-> 6）-α-Gal-OC6H4NO2-p，β-Gal-（1-> 6）-β-Gal-OC6H4NO2-p，β-Gal-（1-> 6） -alpha-GalNAc-OC6H4NO2-p，beta-Gal-（1-> 6）-beta-GalNAc-OC6H4NO2-p，beta-Gal-（1-> 6）-alpha-GlcNAc-OC6H4NO2-p β-Gal-（1-> 6）-β-GlcNAc-OC6H4NO2-p。该酶对α-糖苷受体显示出比相应的β-糖苷受体高得多的转糖基化活性。来自环状芽孢杆菌ATCC 31382的β-D-半乳糖苷酶的区域选择性在很大程度上取决于受体的性质。当

  DOI：

  10.1016/s0008-6215(99)00303-1

文献信息

• Methods and formulations for reducing circulating antibodies
  申请人：——

  公开号：US20010010818A1

  公开（公告）日：2001-08-02

  The invention provides methods for reducing circulating levels of antibodies, particularly disease-associated antibodies. The methods entail administering effective amounts of epitope-presenting carriers to an individual. In other embodiments, ex vivo methods for reducing circulating levels of antibodies are provided which employ epitope-presenting carriers.

  本发明提供了降低循环抗体水平的方法，特别是疾病相关抗体。该方法包括向个体施用有效剂量的表位呈现载体。在其他实施例中，本发明提供了利用表位呈现载体的体外降低循环抗体水平的方法。
• Conjugates comprising galactose alpha 1,3 galactosyl epitopes and methods of using same
  申请人：——

  公开号：US20020160964A1

  公开（公告）日：2002-10-31

  This invention provides conjugates useful for xenotransplantation which comprise a galactose &agr;1,3 galactosyl (&agr;Gal) epitope conjugated to a valency platform molecule, preferably a chemically defined valency platform molecule which allows precise valency. The invention also provides compositions comprising these conjugates, and methods (such as methods for inducing tolerance) using these conjugates and compositions.

  该发明提供了用于异种移植的共轭物，其包括将半乳糖α1,3半乳糖基（αGal表位）与价数平台分子结合而成，优选为化学定义的价数平台分子，以允许精确的价数。该发明还提供了包括这些共轭物的组合物，以及使用这些共轭物和组合物的方法（例如诱导耐受的方法）。
• Substrate specificity and other properties of the β-d- galactosidase from Aspergillus niger
  作者：Donald E. Sykes、Saeed A. Abbas、Joseph J. Barlow、Khushi L. Matta

  DOI：10.1016/s0008-6215(00)90960-1

  日期：1983.5

  beta-D-Galactosidase from Aspergillus niger was purified by conventional techniques, including the repeated use of chromatography on hydroxylapatite. The final preparation represented a 112-fold purification, with a 22% yield. The specific activity of the purified enzyme was 72 mumol of D-galactose released/min/mg of protein, using p-nitrophenyl beta-D-galactopyranoside as the substrate. The substrate specificity of the enzyme was studied by using saccharides having structural linkages similar to those found in naturally occurring glycoconjugates. At substrate concentrations of 5mM, the beta-D-galactosidase efficiently hydrolyzed beta-Gal-1 leads to OC6H4NO2-p, beta-Gal-(1 leads to 3)-Gal, beta-Gal-(1 leads to 3)-beta-Gal-1 leads to OC6H4NO2-p, and beta-Gal-(1 leads to 3)-alpha-Gal-1 leads to OC6H4NO2-p, at rates of 63, 53, 65, and 29 mumol/min/mg of protein, respectively. Slower hydrolysis was observed for beta-Gal-(1 leads to 4)-beta-Glc, beta-Gal-(1 leads to 4)-beta-GlcNAc-1 leads to OC6H4NO2-p, and beta-Gal-(1 leads to 6)-beta-GlcNAc-1 leads to OC6H4NO2-p, with rates of 10, 13 and 9 mumol/min/mg of protein, respectively. Poorly hydrolyzed, at rates 1/300th of that of beta-Gal-1 leads to OC6H4NO2-p, were synthetic substrates having D-galactose attached beta-(1 leads to 3)- to either GalNAc or GlcNAc. The Km value for beta-D-galactosidase with beta-Gal-(1 leads to 4)-beta-GlNAc-1 leads to OC6H4NO2-p was approximately 20 times that with beta-Gal-1 leads to OC6H4NO2-p. The beta-D-galactosidase of A. niger has a molecular weight of 300,000, as demonstrated by gel-filtration chromatography. Sodium dodecyl sulfate-poly(acrylamide)-gel electrophoresis indicated a single subunit having a molecular weight of 130,000.
• CONJUGATES COMPRISING GALACTOSE ALPHA 1,3 GALACTOSYL EPITOPES AND METHODS OF USING SAME
  申请人：LA JOLLA PHARMACEUTICAL

  公开号：EP1137652A2

  公开（公告）日：2001-10-04
• US6399578B1
  申请人：——

  公开号：US6399578B1

  公开（公告）日：2002-06-04