(6-氨基己基)三甲基铵溴化物氢溴酸盐 | 33968-67-1

• 分子结构分类: 有机化合物 - 有机氮化合物
• 中文名称: (6-氨基己基)三甲基铵溴化物氢溴酸盐
• 中文别名: 6-氨基-N，N，N-三甲基-1-己酮最小溴化物氢溴化物；盐酸考来维仑杂质
• 英文名称: (6-aminohexyl)trimethylammonium bromide hydrobromide
• 英文别名: AHTA；6-aminohexyl(trimethyl)azanium;bromide;hydrobromide
• CAS: 33968-67-1
• 化学式: BrH*Br*C₉H₂₃N₂
• 分子量: 320.111
• InChiKey: NIELYIRFOUAOEZ-UHFFFAOYSA-M

物化性质

• 熔点：
  62-64°C
• 溶解度：
  DMSO（少许）、甲醇（少许）、水（少许）

计算性质

• 辛醇/水分配系数(LogP)：
  -1.21
• 重原子数：
  13
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  26
• 氢给体数：
  2
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  (6-氨基己基)三甲基铵溴化物氢溴酸盐 在 氢溴酸 、 N,N'-二环己基碳二亚胺 作用下， 以 溶剂黄146 、 N,N-二甲基甲酰胺 为溶剂， 生成
  参考文献：
  名称：

  Preparation and Properties of Acetylcholinesterase from the Sea MusselMytilus edulis

  摘要：

  The large-scale isolation of an acetylcholinesterase from the haemolymph of the sea mussel mytilus edulis by means of fractional (NH4)2SO4 precipitation, affinity chromatography and isoelectric focusing is described. The yield is about 20% of the initial enzyme activity with a specific activity of 1727 nkat/mg protein. Purification steps are followed by disc electrophoresis, analytical isoelectric focusing and immunoelectrophoresis, showing the enzyme to be homogeneous with an isoelectric point of 4.81 +/- 0.02 and to have an apparent molecular weight of 245,000, which is composed by six equal subunits as judged by C- and N-terminal amino acid analysis. The acetylcholinesterase is a metalloprotein containing three Fe2 ions per subunit (molecular weight 40625); this consists of 351 amino acid and six sugar residues, but contains no sialic acid. As calculated from CD data, the enzyme has about 55% helical structure.

  DOI：

  10.1515/bchm2.1978.359.2.1783

文献信息

• [EN] DEPALMITOYLATING COMPOSITIONS AND THE USE THEREOF<br/>[FR] COMPOSITIONS DE DÉPALMITYLATION ET LEUR UTILISATION
  申请人：UNIV CALIFORNIA

  公开号：WO2021030703A1

  公开（公告）日：2021-02-18

  Disclosed herein, inter alia, are depalmitoylating compounds, compositions, and methods of use thereof.

  本文披露了脱棕榈酰化化合物、组合物及其使用方法。
• Preparation and Properties of Acetylcholinesterase from the Sea Mussel<i>Mytilus edulis</i>
  作者：Herbert ENGELS、Jutta NEEF、Dettmar von WACHTENDONK

  DOI：10.1515/bchm2.1978.359.2.1783

  日期：1978.1

  The large-scale isolation of an acetylcholinesterase from the haemolymph of the sea mussel mytilus edulis by means of fractional (NH4)2SO4 precipitation, affinity chromatography and isoelectric focusing is described. The yield is about 20% of the initial enzyme activity with a specific activity of 1727 nkat/mg protein. Purification steps are followed by disc electrophoresis, analytical isoelectric focusing and immunoelectrophoresis, showing the enzyme to be homogeneous with an isoelectric point of 4.81 +/- 0.02 and to have an apparent molecular weight of 245,000, which is composed by six equal subunits as judged by C- and N-terminal amino acid analysis. The acetylcholinesterase is a metalloprotein containing three Fe2 ions per subunit (molecular weight 40625); this consists of 351 amino acid and six sugar residues, but contains no sialic acid. As calculated from CD data, the enzyme has about 55% helical structure.