7-二乙氨基-3-[N-(2-马来酰亚胺)氨基甲酰基]香豆素
![7-二乙氨基-3-[N-(2-马来酰亚胺)氨基甲酰基]香豆素结构式](https://image.chemsrc.com/caspic/226/156571-46-9.png)
7-二乙氨基-3-[N-(2-马来酰亚胺)氨基甲酰基]香豆素结构式
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常用名 | 7-二乙氨基-3-[N-(2-马来酰亚胺)氨基甲酰基]香豆素 | 英文名 | 7-Diethylamino-3-[N-(2-maleimidoethyl)carbamoyl]coumarin |
|---|---|---|---|---|
| CAS号 | 156571-46-9 | 分子量 | 383.39800 | |
| 密度 | 1.346g/cm3 | 沸点 | 690.5ºC at 760mmHg | |
| 分子式 | C20H21N3O5 | 熔点 | N/A | |
| MSDS | 中文版 美版 | 闪点 | 371.4ºC | |
| 符号 |
GHS07 |
信号词 | Warning |
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A fluorescent sensor of the phosphorylation state of nucleoside diphosphate kinase and its use to monitor nucleoside diphosphate concentrations in real time.
Biochemistry 40(16) , 5087-94, (2001) A sensor for purine nucleoside diphosphates in solution based on nucleoside diphosphate kinase (NDPK) has been developed. A single cysteine was introduced into the protein and labeled with the environmentally sensitive fluorophore, N-[2-(iodoacetamido)ethyl]-... |
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A new method for the time-resolved measurement of phosphate release in permeabilized muscle fibers.
Biophys. J. 68(4 Suppl) , 191S-192S; discussion 192S-193S, (1995) A new method for the measurement of phosphate release in contracting and relaxed permeabilized muscle fibers is described. The assay is based on a genetically engineered phosphate-binding protein labeled with a coumarin fluorescent probe, which binds inorgani... |
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Development of fluorescent biosensors for probing the function of motor proteins.
Mol. Biosyst. 3(4) , 249-56, (2007) Biosensors are becoming widely used both in basic research and in screening assays and reagentless sensors with fluorescent reporter groups attached to proteins form one class. This article describes the development of sensors for two small molecules, driven ... |
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Site-specific labeling of T7 DNA polymerase with a conformationally sensitive fluorophore and its use in detecting single-nucleotide polymorphisms.
Anal. Biochem. 384(1) , 136-44, (2009) Like most enzymes, DNA polymerases undergo a large conformational change on the binding of a correct nucleotide. To determine how the conformational change contributes to substrate specificity, we labeled the T7 DNA polymerase with a conformationally sensitiv... |
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The interaction between rac1 and its guanine nucleotide dissociation inhibitor (GDI), monitored by a single fluorescent coumarin attached to GDI.
Biochemistry 38(21) , 6879-86, (1999) The interaction of rac with guanine nucleotide dissociation inhibitor protein (rhoGDI) is described, using GDI fluorescently labeled on its single cysteine with N-[2-(1-maleimidyl)ethyl]-7-diethylaminocoumarin-3-carboxamide (MDCC). The labeled GDI shows a 70%... |
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Crystal structure of phosphate binding protein labeled with a coumarin fluorophore, a probe for inorganic phosphate.
Biochemistry 37 , 10381, (1998) Crystal structures are presented for the A197C mutant of Escherichia coli phosphate binding protein (PBP) and the same mutant labeled at Cys197 with N-[2-(1-maleimidyl)ethyl]-7-(diethylamino)coumarin-3-carboxamide (MDCC). Both proteins are complexed with inor... |
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Rate of phosphate release after photoliberation of adenosine 5'-triphosphate in slow and fast skeletal muscle fibers.
Biophys. J. 75(5) , 2389-401, (1998) Inorganic phosphate (Pi) release was determined by means of a fluorescent Pi-probe in single permeabilized rabbit soleus and psoas muscle fibers. Measurements of Pi release followed photoliberation of approximately 1.5 mM ATP by flash photolysis of NPE-caged ... |
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ATPase kinetics on activation of rabbit and frog permeabilized isometric muscle fibres: a real time phosphate assay.
J. Physiol. 501 ( Pt 1) , 125-48, (1997) 1. The rate of appearance of inorganic phosphate (Pi) and hence the ATPase activity of rabbit psoas muscle in single permeabilized muscle fibres initially in rigor was measured following laser flash photolysis of the P3-1-(2-nitrophenyl)ethyl ester of ATP (NP... |
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Phosphate binding protein as the biorecognition element in a biosensor for phosphate.
Sens. Actuators B Chem. 97(1) , 81-9, (2004) This work explores the potential use of a member of the periplasmic family of binding proteins, the phosphate binding protein (PBP), as the biorecognition element in a sensing scheme for the detection of inorganic phosphate (Pi). The selectivity of this prote... |
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Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.
Proc. Natl. Acad. Sci. U. S. A. 110(46) , E4289-97, (2013) The complex kinetics of Pi and ADP release by the chaperonin GroEL/GroES is influenced by the presence of unfolded substrate protein (SP). Without SP, the kinetics of Pi release are described by four phases: a "lag," a "burst" of ATP hydrolysis by the nascent... |