Sodium methanesulfinate
Sodium methanesulfinate structure
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Common Name | Sodium methanesulfinate | ||
|---|---|---|---|---|
| CAS Number | 20277-69-4 | Molecular Weight | 102.088 | |
| Density | N/A | Boiling Point | 256.4ºC at 760 mmHg | |
| Molecular Formula | CH3NaO2S | Melting Point | 222-226 °C (dec.)(lit.) | |
| MSDS | Chinese USA | Flash Point | 108.9ºC | |
| Symbol |
GHS07 |
Signal Word | Warning | |
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Reactivity of C-terminal cysteines with HNO.
Biochemistry 53(22) , 3689-98, (2014) Nitroxyl (HNO), a potential heart failure therapeutic, is known to target cysteine residues to form sulfinamides and/or disulfides. Because HNO-derived modifications may depend on their local environment, we have investigated the reactivity of HNO with cystei... |
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Colorimetric assay for methanesulfinic acid in biological samples.
Anal. Biochem. 163(1) , 67-73, (1987) We describe a simple colorimetric method to measure 30 to 300 microM concentrations of sulfinic acids in biologic samples. The procedure employs the coupling reaction of an aromatic diazonium salt (Ar--N = N+) with the sulfinic acids (RSOOH) to produce a colo... |
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Modifiers of mercaptopyruvate sulfurtransferase catalyzed conversion of cyanide to thiocyanate in vitro.
J. Biochem. Toxicol. 7(2) , 65-72, (1992) The enzyme mercaptopyruvate sulfurtransferase appears to play an important role in the in vivo detoxification of cyanide. It does so by transferring sulfur to cyanide to produce thiocyanate, which is less toxic and may be excreted through the kidney. Several ... |
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Determination of low-molecular-weight thiols using monobromobimane fluorescent labeling and high-performance liquid chromatography.
Meth. Enzymol. 143 , 85, (1987)
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Oxidation of DMSO and methanesulfinic acid by the hydroxyl radical.
Free Radic. Biol. Med. 18(2) , 271-7, (1995) The quantitation of methanesulfinic acid, the reaction product of dimethylsulfoxide oxidation by the hydroxyl radical, has been reported as a useful tool for the detection of this radical. The present report describes two HPLC methods for determination of met... |
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Quantitative effects of iron chelators on hydroxyl radical production by the superoxide-driven fenton reaction.
Free Radic. Res. Commun. 8(2) , 101-6, (1990) Iron bound to certain chelators is known to promote the conversion of superoxide radicals (O2-) to hydroxyl radicals (HO.) by the superoxide-driven Fenton reaction. The production of HO. by various iron chelates was studied using the reaction of dimethyl sulf... |
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Reevaluating the role of 1,10-phenanthroline in oxidative reactions involving ferrous ions and DNA damage.
Biochim. Biophys. Acta 1675(1-3) , 46-53, (2004) It is widely believed that the iron chelator 1,10-phenanthroline (phen) is able to fully block the Fenton reaction by forming a complex (Fe(phen)3(2+), also known as ferroin) that cannot react with H2O2. We observed that phen cannot fully prevent 2-deoxyribos... |
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Quantitation of the hydroxyl radical by reaction with dimethyl sulfoxide.
Arch. Biochem. Biophys. 278(2) , 478-81, (1990) This investigation was conducted to validate the use of dimethyl sulfoxide (DMSO) as a quantitative molecular probe for the generation of hydroxyl radicals (HO.) in aqueous systems. Reaction of HO. with DMSO produces methane sulfinic acid as a primary product... |
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Hydroxyl radical generation by postischemic rat kidney slices in vitro.
Free Radic. Biol. Med. 9(1) , 67-77, (1990) To quantitate the formation of hydroxyl radicals (HO.) in ischemia and reoxygenation, dimethyl sulfoxide (DMSO) was added to "trap" evolving HO. in normal, in ischemic, and in ischemic and reoxygenated rat kidney slices, incubated in short-term organ culture ... |
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Synthesis and application of a Sec2-containing oligopeptide for method evaluation purposes in selenium speciation.
Talanta 99 , 186-93, (2012) Sec(2)-containing oligopeptide was synthesized directly from Sec(2) with the traditional liquid phase peptide synthesis without addressing the usually applied and complex solid phase (SPPS) protocol driving through a protected Sec residue and site-oriented ox... |