4-amino-2,6-dichlorophenyl phosphate | 124219-30-3

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磷酸及其衍生物
• 英文名称: 4-amino-2,6-dichlorophenyl phosphate
• 英文别名: (4-Amino-2,6-dichlorophenyl) dihydrogen phosphate
• CAS: 124219-30-3
• 化学式: C₆H₆Cl₂NO₄P
• 分子量: 257.998
• InChiKey: WRDYCKRALGQXOH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  14
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  92.8
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  4-amino-2,6-dichlorophenyl phosphate 在 magnesium chloride bovine serum albumine 、 Tris buffer 作用下， 生成 2,6-二氯-4-氨基苯酚
  参考文献：
  名称：

  Theory and Practice of Enzyme Bioaffinity Electrodes. Direct Electrochemical Product Detection

  摘要：

  The use of enzyme labeling techniques to convert biorecognition events into high sensitivity electrochemical signals may follow two different strategies. One, in which the current is the electrocatalytic response of a redox couple serving as cosubstrate to a redox enzyme label and another that consists in the detection of an electrochemically active product of the enzyme label. The theoretical relationships that link, in the latter case, the electrochemical current response to the amount of recognized labeled target analyte are established for steady-state diffusion-convection chronoamperometric regimes. Two governing parameters thus emerge. One measures the Michaelis-Menten competition in the enzyme kinetics. The other characterizes the competition between the enzymatic kinetics and the diffusion of the substrate. The electrochemical response is finally related to the labeled target analyte concentration in solution through the recognition isotherm. The direct electrochemical product detection thus provides a route to the characteristics of the recognition isotherm, which serves as a calibration curve in analytical applications. The establishment of further theoretical relationships allows one to surmise the increase in sensitivity that may be obtained by using cyclic voltammetry instead of steady-state chronoamperometry in standard electrochemical cells or by accumulation of the enzyme-product in cells of small volume/surface ratios. The theoretical predictions are tested with the example of the avidin-biotin recognition process in a system that involves alkaline phosphatase as enzyme label and 4-amino-2,6-dichlorophenyl phosphate as substrate, generating 4-amino-2,6-dichlorophenol as electrochemically active product. The advantages of the dichloro-substitution are discussed. The theoretical analysis is a requisite for a rational and realistic discussion of the analytical performances of the steady-state chronoamperometric and cyclic voltammetric approaches. These are shown to compare favorably with the best heterogeneous bioaffinity assays so far reported.

  DOI：

  10.1021/ja7102845
• 作为产物：
  描述：

  (4-nitro-2,6-dichlorophenyl)-dibenzyl phosphate 在 Lindlar's catalyst 氢气 作用下， 以 甲醇 为溶剂， 20.0 ℃ 、100.0 kPa 条件下， 反应 12.0h， 以67%的产率得到4-amino-2,6-dichlorophenyl phosphate
  参考文献：
  名称：

  Theory and Practice of Enzyme Bioaffinity Electrodes. Direct Electrochemical Product Detection

  摘要：

  The use of enzyme labeling techniques to convert biorecognition events into high sensitivity electrochemical signals may follow two different strategies. One, in which the current is the electrocatalytic response of a redox couple serving as cosubstrate to a redox enzyme label and another that consists in the detection of an electrochemically active product of the enzyme label. The theoretical relationships that link, in the latter case, the electrochemical current response to the amount of recognized labeled target analyte are established for steady-state diffusion-convection chronoamperometric regimes. Two governing parameters thus emerge. One measures the Michaelis-Menten competition in the enzyme kinetics. The other characterizes the competition between the enzymatic kinetics and the diffusion of the substrate. The electrochemical response is finally related to the labeled target analyte concentration in solution through the recognition isotherm. The direct electrochemical product detection thus provides a route to the characteristics of the recognition isotherm, which serves as a calibration curve in analytical applications. The establishment of further theoretical relationships allows one to surmise the increase in sensitivity that may be obtained by using cyclic voltammetry instead of steady-state chronoamperometry in standard electrochemical cells or by accumulation of the enzyme-product in cells of small volume/surface ratios. The theoretical predictions are tested with the example of the avidin-biotin recognition process in a system that involves alkaline phosphatase as enzyme label and 4-amino-2,6-dichlorophenyl phosphate as substrate, generating 4-amino-2,6-dichlorophenol as electrochemically active product. The advantages of the dichloro-substitution are discussed. The theoretical analysis is a requisite for a rational and realistic discussion of the analytical performances of the steady-state chronoamperometric and cyclic voltammetric approaches. These are shown to compare favorably with the best heterogeneous bioaffinity assays so far reported.

  DOI：

  10.1021/ja7102845

文献信息

• Method and test composition for determination of enzyme activity
  申请人：Kyowa Medex Co. Ltd.

  公开号：EP0317243A2

  公开（公告）日：1989-05-24

  Disclosed is a method for determination of an activity of γ-glutamyl transpeptidase, leucine aminopeptidase, alanine aminopeptidase, cystine aminopeptidase, X factor as a coagulation factor, thrombin, plasmin of plasminogen series, kallikrein, chymotrypsin, alkali phosphatase, N-acetyl glucosaminase and amylase, by allowing a particular substrate to act on the enzyme to thereby form an enhancer; oxidizing a chromogen by an oxidase in the presence of the enhancer and oxygen to form a pigment; and determining the pigment. Also disclosed is a test composition for carrying out the determination.

  本发明公开了一种测定γ-谷氨酰转肽酶、亮氨酸氨肽酶、丙氨酸氨肽酶、胱氨酸氨肽酶、作为凝血因子的 X 因子、凝血酶、纤溶酶原系列的纤溶酶、胰凝乳蛋白酶、糜蛋白酶、碱式磷酸酶、N-乙酰葡糖胺酶和淀粉酶活性的方法，其方法是让特定的底物作用于酶，从而形成增强剂；在增强剂和氧气存在的情况下，用氧化酶氧化色原，形成色素；以及测定色素。还公开了一种用于进行测定的试验组合物。