2-氯-4-硝基苯-alpha-L-岩藻糖苷 | 157843-41-9

• 物质功能分类: 原料药 - 抗生素类药物 - 氨基糖苷类药
• 分子结构分类: 有机化合物 - 有机氧化合物
• 中文名称: 2-氯-4-硝基苯-alpha-L-岩藻糖苷
• 中文别名: 2-氯-4-硝基苯-a-L-岩藻糖苷；2-氯-对硝基苯-a-L-岩藻糖苷；2-氯-4-硝基苯-O-氧代三羟基环氧戊烷；2-氯-4-硝基苯基-Alpha-L-岩藻糖苷；2-氯-4-硝基苯基-L-岩藻糖苷；2-氯-4-硝基苯-A-L-岩藻糖苷；2-氯-4-硝基苯-α-L-岩藻糖苷；CNP-AFU
• 英文名称: 2-chloro-4-nitrophenyl α-L-fucopyranoside
• 英文别名: 2-chloro-4-nitrobenzene-α-L-fucoside；2C4NP-α-L-Fuc；CNPF；2-Chloro-4-nitrophenyl-alpha-L-fucopyranoside；(2S,3S,4R,5S,6S)-2-(2-chloro-4-nitrophenoxy)-6-methyloxane-3,4,5-triol
• CAS: 157843-41-9
• 化学式: C₁₂H₁₄ClNO₇
• 分子量: 319.699
• InChiKey: QURSGHQPKUXLAD-MOBXTKCLSA-N

物化性质

• 熔点：
  137-139°C
• 沸点：
  527.3±50.0 °C(Predicted)
• 密度：
  1.584±0.06 g/cm3(Predicted)
• 溶解度：
  甲醇

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  21
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  125
• 氢给体数：
  3
• 氢受体数：
  7

安全信息

• 安全说明：
  S24/25,S26,S36/37/39
• 海关编码：
  2932999099
• 储存条件：
  -20°C

制备方法与用途

性状

2-氯-4-硝基苯-α-L-岩藻糖苷（CNP-AFU）是一种白色粉末。

用途

2-氯-4-硝基苯-α-L-岩藻糖苷主要用于检测血清中α-L-岩藻糖苷酶（AFU）的含量，并用于研发和大量制备AFU检测试剂。

作用原理

血清中的AFU会将底物转化为2-氯-4-硝基苯（CNP），在405nm波长下测量每分钟吸光度的变化率（ΔA/min），以此来计算其活性。

优势

1. 水溶性好；
2. 灵敏度高；
3. 线性范围宽；
4. 稳定性强。

生物活性

CNP-AFU是α-L-岩藻糖苷酶（AFU）的底物。

反应信息

• 作为反应物：
  描述：

  2-氯-4-硝基苯-alpha-L-岩藻糖苷 在 Sulfolobus solfataricus α-L-fucosidase 作用下， 生成 2-氯-4-硝基苯酚
  参考文献：
  名称：

  β-Glycosyl Azides as Substrates for α-Glycosynthases: Preparation of Efficient α-L-Fucosynthases

  摘要：

  Fucose-containing oligosaccharides play a central role in physio-pathological events, and fucosylated oligosaccharides have interesting potential applications in biomedicine. No methods for the large-scale production of oligosaccharides are currently available, but the chemo-enzymatic approach is very promising. Glycosynthases, mutated glycosidases that synthesize oligosaccharides in high yields, have been demonstrated to be an interesting alternative. However, examples of glycosynthases available so far are restricted to a limited number of glycosidases families and to only one retaining alpha-glycosynthase. We show here that new mutants of two alpha-L-fucosidases are efficient alpha-L-fucosynthases. The approach shown utilized beta-L-fucopyranosyl azide as donor substrate leading to transglycosylation yields up to 91%. This is the first method exploiting a beta-glycosyl azide donor for alpha-glycosynthases; its applicability to the glycosynthetic methodology in a wider perspective is presented.

  DOI：

  10.1016/j.chembiol.2009.09.013
• 作为产物：
  描述：

  2-chloro-4-nitrophenyl 3,4-di-O-tert-butyldimethylsilyl-α-L-fucopyranoside 在 氟化氢吡啶 作用下， 以 吡啶 、 乙腈 为溶剂， 反应 20.0h， 以68%的产率得到2-氯-4-硝基苯-alpha-L-岩藻糖苷
  参考文献：
  名称：

  Synthesis of 2-chloro-4-nitrophenyl α-l-fucopyranoside: a substrate for α-l-fucosidase (AFU)

  摘要：

  An effective method to prepare the substrate of alpha-L-fucosidase (AFU) is described. Ethyl 1-thiofucoside with a free 2-OH group was used as the glycosyl donor, and there was found no self-condensed side product. The use of the HF . pyridine reagent to remove the silyl protecting group in the last step afforded a target molecule of high purity. (C) 2003 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/s0008-6215(03)00244-1

文献信息

• 一种2-氯-4-硝基苯-α-L-岩藻糖苷的制备方法
  申请人：上海瀚诺威生物科技有限公司

  公开号：CN113480584A

  公开（公告）日：2021-10-08

  本发明公开了一种2‑氯‑4‑硝基苯‑α‑L‑岩藻糖苷的制备方法，属于体外诊断领域。本发明以L‑岩藻糖为起始原料，通过乙酰化反应，制得1,2,3,4‑四乙酰基‑α‑L‑岩藻糖，再与2‑氯‑4‑硝基苯酚发生糖苷化反应，制得2‑氯‑4‑硝基苯‑2,3,4‑三乙酰基‑α‑L‑岩藻糖苷，其中，所述催化剂选择三氟甲磺酸三甲基硅酯或三氟化硼乙醚；最后进行脱乙酰基反应，制得2‑氯‑4‑硝基苯‑α‑L‑岩藻糖苷。本发明方法反应路线较短，通过三步反应制得最终产品；且以L‑岩藻糖为原料，起始原料价格相对便宜，2‑氯‑4‑硝基苯酚用量明显减少；后处理过程简单且反应重现性好，可实现工业化生产。
• SERUM FUCOSIDASE DETECTION KIT
  申请人：Ningbo Medical System Biotechnology Co. Ltd.

  公开号：EP3208613A1

  公开（公告）日：2017-08-23

  Disclosed is a serum fucosidase detection kit. The kit comprises a reagent 1 and a reagent 2, wherein the reagent 1 consists of 50-500 mmol/L of a buffer (pH 4.0-4.5), 1-50 g/L of a surfactant, 1-20 g/L of an anti-interference agent and 0.1-100 g/L of a preservative; and the reagent 2 consists of 50-500 mmol/L of a buffer (pH 7.0-7.5), 2-60 g/L of glucose, 1-20 KU/L of hexokinase, 1-20 KU/L of glucose-6-phosphate dehydrogenase, 0.3-5 g/L of magnesium sulfate, 0.2-5 g/L of a substrate, 1-100 mmol/L of a stabilizer, 0.1-40 g/L of a protective agent and 0.1-100 g/L of a preservative. The kit solves the problems of the poor substrate stability, the poor anti-interference capacity and the low sensitivity which exist universally.

  本发明公开了一种血清岩藻糖苷酶检测试剂盒。该试剂盒包括试剂 1 和试剂 2，其中试剂 1 由 50-500 mmol/L 的缓冲液（pH 4.0-4.5）、1-50 g/L 的表面活性剂、1-20 g/L 的抗干扰剂和 0.1-100 g/L 的防腐剂组成；试剂 2 由 50-500 mmol/L 的缓冲液（pH 7.0-7.5）、葡萄糖 2-60 g/L、己糖激酶 1-20 KU/L、葡萄糖-6-磷酸脱氢酶 1-20 KU/L、硫酸镁 0.3-5 g/L、底物 0.2-5 g/L、稳定剂 1-100 mmol/L、保护剂 0.1-40 g/L 和防腐剂 0.1-100 g/L。该试剂盒解决了普遍存在的底物稳定性差、抗干扰能力差和灵敏度低的问题。
• Cleavage of fucose in N-glycans
  申请人：New England Biolabs, Inc.

  公开号：US10260056B2

  公开（公告）日：2019-04-16

  Provided herein is an α-fucosidase that can cleave a conjugate comprising an N-glycan and a label where the label is added by amine reactive chemistry. The α-fucosidase also has an accelerated reaction time using Schiff base labeled N-glycans compared with bovine kidney fucosidase. A reaction mix, enzyme mix and kit comprising the α-fucosidase are provided, as well as a method for analyzing glycoproteins. The α-fucosidase finds particular use in analyzing the N-glycans of therapeutic glycoproteins.

  本文提供了一种α-岩藻糖苷酶，它可以裂解由 N-聚糖和标签组成的共轭物，其中标签是通过胺反应化学反应添加的。与牛肾岩藻糖苷酶相比，α-岩藻糖苷酶在使用希夫碱标记的 N-聚糖时反应时间更快。本研究提供了包含 α-岩藻糖苷酶的反应混合物、酶混合物和试剂盒，以及分析糖蛋白的方法。α-岩藻糖苷酶特别适用于分析治疗性糖蛋白的 N-聚糖。
• Expression, Purification and Characterization of Human α-<scp>l</scp>-Fucosidase
  作者：Sheng-Wen Liu、Yaw-Kuen Li

  DOI：10.1002/jccs.200900126

  日期：2009.8

  Abstractα‐l‐Fucosidases (EC 3.2.1.51) are exo‐glycosidases. On the basis of the multi‐alignment of amino acid sequence, α‐l‐fucosidases were classified into two families of glycoside hydrolases, GH‐29 and GH‐95. They are responsible for the removal of l‐fucosyl residues from the non‐reducing end of glycoconjugates. Deficiency of α‐l‐fucosidase results in Fucosidosis due to the accumulation of fucose‐containing glycolipids, glycoproteins and oligosaccharides in various tissues. Recent studies discovered that the fucosylation levels are increased on the membrane surfaces of many carcinomas, indicating the biological function of α‐l‐fucosidases may relate to this abnormal cell physiology. Although the gene of human α‐l‐fucosidase (h‐fuc) was cloned, the recombinant enzyme has rarely been overexpressed as a soluble and active from. We report herein that, with carefully control on the growing condition, an active human α‐l‐fucosidases (h‐Fuc) was successfully expressed in Escherichia coli for the first time. After a series steps of ion‐exchange and gel‐filtration chromatographic purification, the recombinant h‐Fuc with 95% homogeneity was obtained. The molecular weight of the enzyme was analyzed by SDS‐PAGE (∼50 kDa) and confirmed by ESI mass (50895 Da). The recombinant h‐Fuc was stable up to 55 °C with incubation at pH 6.8 for 2 h; the optimum temperature for h‐Fuc is approximately 55 °C. The enzyme was stable at pH 2.5–7.0 for 2 h; the enzyme activity decreased greatly for pH greater than 8.0 or less than 2.0. The Km and kcat values of the recombinant h‐Fuc (at pH 6.8) were determined to be 0.28 mM and 17.1 s−1, respectively. The study of pH‐dependent activity showed that the recombinant enzyme exhibited optimum activity at two regions near at pH 4.5 and pH 6.5. These features of the recombinant h‐Fuc are comparable to the native enzyme purified directly from human liver. Studies on the transfucosylation and common intermediate of the enzymatic reaction by NMR support that h‐Fuc functions as a retaining enzyme catalyzing the hydrolysis of substrate via a two‐step, double displacement mechanism.
• USE OF SUBSTRATES AS PHARMACOLOGICAL CHAPERONES
  申请人：Amicus Therapeutics, Inc.

  公开号：EP2137204A1

  公开（公告）日：2009-12-30