4-(2-Pyridylazo)resorcinol (PAR) is a monosodium salt(1), dibasic acid that forms the protonated complexes with most metal ions.
Application
4-(2-Pyridylazo)resorcinol (PAR) serves as a metallochromic indicator and is suitable as a chromogenic agent for the quantitative determination of over 50 elements.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
dust mask type N95 (US), Eyeshields, Gloves
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Dalton transactions (Cambridge, England : 2003), 39(5), 1366-1374 (2010-01-28)
Literature reports of the efficacy of para-sulfonatocalix[6]- and calix[8]-arenes as U(vi) complexants indicated that they might be useful for in vivo chelation of the novel therapeutic alpha-emitter (230)U. We have studied the complexation of U(vi) with para-sulfonatocalix[6]arene and para-sulfonatocalix[8]arene by
In this study, X-ray photoelectron spectroscopy (XPS) was used to study chitosan-graphene oxide (chitosan-GO) incorporated with 4-(2-pyridylazo)resorcinol (PAR) and cadmium sulfide quantum dot (CdS QD) composite thin films for the potential optical sensing of cobalt ions (Co2+). From the XPS
Journal of hazardous materials, 171(1-3), 1133-1138 (2009-08-04)
A procedure for simultaneous separation/preconcentration of copper, zinc, cadmium, and nickel in water samples, based on cloud point extraction (CPE) as a prior step to their determination by inductively coupled plasma optic emission spectrometry (ICP-OES), has been developed. The analytes
Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 32(3), 521-532 (2019-02-14)
The biosynthesis of the dinuclear metal cluster at the active sites of the [NiFe]-hydrogenase enzymes is a multi-step process executed by a suite of accessory proteins. Nickel insertion during maturation of Escherichia coli [NiFe]-hydrogenase 3 is achieved by the metallochaperones
In this study, three synthetic zinc-chelating peptides (ZCPs) derived from sea cucumber hydrolysates with limited or none of the common metal-chelating amino-acid residues were analyzed by flame atomic absorption spectroscopy, circular dichroism spectroscopy, size exclusion chromatography, zeta-potential, Fourier transform infrared
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