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succinimido phenylcarbamate | 23583-11-1

中文名称
——
中文别名
——
英文名称
succinimido phenylcarbamate
英文别名
N-[(phenylcarbamoyl)oxy] succinimide;(2,5-dioxopyrrolidin-1-yl) N-phenylcarbamate
succinimido phenylcarbamate化学式
CAS
23583-11-1
化学式
C11H10N2O4
mdl
——
分子量
234.211
InChiKey
RWUGQMFYSYCHIB-UHFFFAOYSA-N
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

物化性质

  • 熔点:
    149-154 °C
  • 密度:
    1.41±0.1 g/cm3(Predicted)

计算性质

  • 辛醇/水分配系数(LogP):
    0.6
  • 重原子数:
    17
  • 可旋转键数:
    3
  • 环数:
    2.0
  • sp3杂化的碳原子比例:
    0.18
  • 拓扑面积:
    75.7
  • 氢给体数:
    1
  • 氢受体数:
    4

安全信息

  • 海关编码:
    2925190090

SDS

SDS:e84b423d65bb8e8360f57fff93544c45
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反应信息

  • 作为反应物:
    描述:
    succinimido phenylcarbamate乙腈 为溶剂, 反应 18.17h, 生成
    参考文献:
    名称:
    衍生,消旋和分析-对映选择性代谢组学的手性氨基酸标准品制备的简便方法。
    摘要:
    开发了一种简单,可控制和可重现的立体异构化方法(消旋和差向异构化),用于从立体异构纯标准品制备规模化α-氨基酸混合物。只需使用消旋标签衍生化您的氨基酸即可,该消旋标签在目标氨基酸的N-末端掺有尿素键,并在高达95°C的高温下孵育一段确定的时间,直至获得目标d-氨基酸水平。研究的外消旋标记是6-氨基喹啉基-N-羟基琥珀酰亚胺基氨基甲酸酯(AQC),氨基苯基-N-羟基琥珀酰亚胺基氨基甲酸酯(AC)和3-氨基吡啶基-N氨基甲酸-羟基琥珀酰亚胺基酯(APC)。采用这种方法,可以在数分钟内或在几分钟内,制备出可立即使用的,量身定制的,手性均匀的13 C和15 N标记的[U - 13 C 15 N]-氨基酸标准品,并具有所需的d-氨基酸百分比。小时不进行样品清理。在95°C下消旋30分钟的消旋时间将导致d-氨基酸水平为1-5%,而在95°C下6 h消旋时间将提供15-30%的d-氨基酸。外消旋化是由于
    DOI:
    10.1021/acs.analchem.9b00666
  • 作为产物:
    描述:
    参考文献:
    名称:
    アミノ官能性化合物の分析方法及び分析試薬
    摘要:
    提供一种简便且高灵敏度地分析样品中包含的氨基官能化合物、肽等氨基官能性化合物的方法。通过使用特定的卡巴酰化合物,如p-三甲基铵苯甲酰-N-羟基琥珀酰亚胺卡巴酰酶碘化物等,标记样品中包含的氨基官能性化合物,提高选择性,从而实现简便且高灵敏度的分析。特别是,可以通过质谱/质谱法等质谱分析方法定量分析目标化合物。此外,还提供用于质谱分析的标记试剂以及可用于这些标记试剂的新化合物。【选择图】无
    公开号:
    JP2016029068A
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文献信息

  • Polymer-von Willebrand factor-conjugates
    申请人:Scheiflinger Friedrich
    公开号:US20060160948A1
    公开(公告)日:2006-07-20
    The present invention relates to a proteinaceous construct (also designated as polymer-VWF-conjugate) comprising plasmatic and/or recombinant von Willebrand factor (VWF), said VWF being bound to at least one physiologically acceptable polymer molecule, as well as to a complex between said proteinaceous construct and at least one factor VIII (FVIII) protein. The physiologically acceptable polymer molecule can be, for instance, polyethylene glycol (PEG) or polysialic acid (PSA). Further the present invention relates to methods for prolonging the in vivo-half-life of VWF or FVIII in the blood of a mammal having a bleeding disorder associated with functional defects of or deficiencies of at least one of FVIII or VWF.
    本发明涉及一种蛋白质构造物(也称为聚合物-VWF-结合物),包括血浆和/或重组的von Willebrand因子(VWF),所述VWF与至少一种生理可接受的聚合物分子结合,以及所述蛋白质构造物与至少一种因子VIII(FVIII)蛋白复合物之间的复合物。生理可接受的聚合物分子可以是聚乙二醇(PEG)或聚唾液酸(PSA)等。此外,本发明还涉及延长具有与FVIII或VWF的功能缺陷或缺陷相关的出血障碍哺乳动物的血液中VWF或FVIII在体内半衰期的方法。
  • Polymer-Von Willebrand Factor-Conjugates
    申请人:Scheiflinger Friedrich
    公开号:US20120135462A1
    公开(公告)日:2012-05-31
    The present invention relates to a proteinaceous construct (also designated as polymer-VWF-conjugate) comprising plasmatic and/or recombinant von Willebrand factor (VWF), said VWF being bound to at least one physiologically acceptable polymer molecule, as well as to a complex between said proteinaceous construct and at least one factor VIII (FVIII) protein. The physiologically acceptable polymer molecule can be, for instance, polyethylene glycol (PEG) or polysialic acid (PSA). Further the present invention relates to methods for prolonging the in vivo-half-life of VWF or FVIII in the blood of a mammal having a bleeding disorder associated with functional defects of or deficiencies of at least one of FVIII or VWF.
    本发明涉及一种蛋白质构建物(也称为聚合物-VWF-共轭物),包括血浆和/或重组von Willebrand因子(VWF),所述VWF与至少一种生理上可接受的聚合物分子结合,以及所述蛋白质构建物与至少一种因子VIII(FVIII)蛋白质的复合物。生理上可接受的聚合物分子可以是聚乙二醇(PEG)或聚唾液酸(PSA)等。此外,本发明还涉及用于延长哺乳动物(具有与FVIII或VWF的功能缺陷或缺乏相关的出血障碍)血液中VWF或FVIII的体内半衰期的方法。
  • METHOD AND APPARATUS FOR ANALYZING AMINOFUNCTIONAL COMPOUND
    申请人:Ajinomoto Co., Inc.
    公开号:EP1750126A1
    公开(公告)日:2007-02-07
    A method and apparatus for analyzing compounds with amino group including various amino acids, derivatives thereof, and amino acid analogues contained in biological organisms far more rapidly and easily with higher sensitivity than conventional methods. A compound with amino group is reacted with a reagent for derivatization to generate a derivative of the compound with amino group represented by the following general formula (I), and then the derivative of the compound with amino group is eluted by liquid chromatography using a stepwise elution means on a concentration gradient. Subsequently, the derivative of the compound with amino group eluted from the liquid chromatography is detected by mass spectrometry. In the formula, Ar1 denotes an optionally substituted hydrocarbon, or a substituent comprising a carbocyclic or heterocyclic ring having an aromaticity, R1 denotes a hydrogen atom, an optionally substituted alkyl group, or a ring forming carbon atom, and R2 denotes an optionally substituted alkyl group, where Ar1 and R1, or R1 and R2 may form a ring with each other.
    一种方法和装置,用于分析生物体内含有的含氨基化合物,包括各种氨基酸、其衍生物和氨基酸类似物,比传统方法更快、更简便、灵敏度更高。将带氨基的化合物与衍生化试剂反应,生成由以下通式(I)表示的带氨基化合物的衍生物,然后用液相色谱法以浓度梯度逐步洗脱的方式洗脱带氨基化合物的衍生物。随后,用质谱法检测从液相色谱法洗脱出的带氨基的化合物衍生物。 式中,Ar1 表示任选取代的烃,或由具有芳香性的碳环或杂环组成的取代基,R1 表示氢原子、任选取代的烷基或形成环的碳原子,R2 表示任选取代的烷基,其中 Ar1 和 R1 或 R1 和 R2 可相互形成环。
  • Activated carbamate reagent as derivatizing agent for amino compounds in high-performance liquid chromatography
    作者:Noriyuki. Nimura、Kazuo. Iwaki、Toshio. Kinoshita、Kazuyoshi. Takeda、Haruo. Ogura
    DOI:10.1021/ac00125a005
    日期:1986.10.1
  • Structure-Based Design of β-Lactamase Inhibitors. 1. Synthesis and Evaluation of Bridged Monobactams
    作者:Ingrid Heinze-Krauss、Peter Angehrn、Robert L. Charnas、Klaus Gubernator、Eva-Maria Gutknecht、Christian Hubschwerlen、Malgosia Kania、Christian Oefner、Malcolm G. P. Page、Satoshi Sogabe、Jean-Luc Specklin、Fritz Winkler
    DOI:10.1021/jm980023c
    日期:1998.10.1
    Bridged monobactams are novel, potent, mechanism-based inhibitors of class C beta-lactamases, designed using X-ray crystal structures of the enzymes. They stabilize the acyl-enzyme intermediate by blocking access of water to the enzyme-inhibitor ester bond. Bridged monobactams are selective class C beta-lactamase inhibitors, with half-inhibition constants as low as 10 nM, and are less effective against class A and class B enzymes (half-inhibition constants > 100 mu M) because of the different hydrolysis mechanisms in these classes of beta-lactamases. The stability of the acyl-enzyme complexes formed with class C beta-lactamases (half-lives up to 2 days were observed) enabled determination of their crystal structures. The conformation of the inhibitor moiety was close to that predicted by molecular modeling, confirming a simple reaction mechanism, unlike those of known beta-lactamase inhibitors such as clavulanic acid and penam sulfones, which involve secondary rearrangements. Synergy between the bridged monobactams and beta-lactamase-labile antibiotics could be observed when such combinations were tested against strains of Enterobacteriaceae that produce large amounts of class C beta-lactamases. The minimal inhibitory concentration of the antibiotic of more than 64 mg/L could be decreased to 0.25 mg/L in a 1:4 combination with the inhibitor.
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