|
Sullivan Reaction
The Sullivan reaction is a chemical test used for detecting the presence of cysteine or cystine in proteins. A red colour appears when a protein with cysteine or cystine is heated with sodium 1,2-naphthoquinone-4-sulfonate ( Folin's reagent) and sodium dithionite Sodium dithionite (also known as sodium hydrosulfite) is a white crystalline powder with a sulfurous odor. Although it is stable in dry air, it decomposes in hot water and in acid solutions. Structure left, 220px, Packing of sodium dithionit ... under alkaline conditions. This was pioneered by the American organic and industrial chemist Eugene Cornelius Sullivan (1872–1962). References Protein methods Chemical tests {{analytical-chemistry-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chemical Test
In chemistry, a chemical test is a qualitative property, qualitative or Quantitative property, quantitative procedure designed to identify, quantify, or characterise a chemical compound or substituent, chemical group. Purposes Chemical testing might have a variety of purposes, such as to: * Determine if, or verify that, the requirements of a specification, regulation, or contract are met * Decide if a new product development program is on track: Demonstrate proof of concept * Demonstrate the utility of a proposed patent * Determine the interactions of a sample with other known substances * Determine the composition of a sample * Provide Technical standard, standard data for other scientific, medical, and Quality assurance functions * Validate suitability for end-use * Provide a basis for Technical communication * Provide a technical means of comparison of several options * Provide evidence in legal proceedings Biochemical tests * Clinistrips quantitatively test for sugar in uri ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cysteine
Cysteine (; symbol Cys or C) is a semiessential proteinogenic amino acid with the chemical formula, formula . The thiol side chain in cysteine enables the formation of Disulfide, disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine are found in nature. LCysteine is a protein monomer in all biota, and D-cysteine acts as a signaling molecule in mammalian nervous systems. Cysteine is named after its discovery in urine, which comes from the urinary bladder or cyst, from Ancient Greek, Greek κύστις ''kýstis'', "bladder". The thiol is susceptible to oxidation to give the disulfide bond, disulfide derivative cystine, which serves an important structural role in many proteins. In this case, the symbol Cyx is sometimes used. The deprotonated form can generally be described by the symbol Cym as well. When used as a food additive, cysteine has the E number E920. Cysteine is Genetic code, encoded by the codo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cystine
Cystine is the oxidized derivative of the amino acid cysteine and has the formula (SCH2CH(NH2)CO2H)2. It is a white solid that is poorly soluble in water. As a residue in proteins, cystine serves two functions: a site of redox reactions and a mechanical linkage that allows proteins to retain their three-dimensional structure. Formation and reactions Structure Cystine is the disulfide derived from the amino acid cysteine. The conversion can be viewed as an oxidation: : Cystine contains a disulfide bond, two amine groups, and two carboxylic acid groups. As for other amino acids, the amine and carboxylic acid groups exist in rapid equilibrium with the ammonium-carboxylate tautomer. The great majority of the literature concerns the ''l,l-''cystine, derived from ''l''-cysteine. Other isomers include ''d,d''-cystine and the meso isomer d,l-cystine, neither of which is biologically significant. Occurrence Cystine is common in many foods such as eggs, meat, dairy products, and whole ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Folin's Reagent
Folin's reagent or sodium 1,2-naphthoquinone-4-sulfonate is a chemical reagent used as a derivatizing agent to measure levels of amines and amino acids. The reagent reacts with them in alkaline solution to produce a fluorescent material that can be easily detected. This should not be confused with Folin-Ciocalteu reagent, that is used to detect phenolic compounds. The Folin reagent can be used with an acidic secondary reagent to distinguish MDMA and related compounds from PMMA and related compounds. See also * Dille–Koppanyi reagent * Froehde reagent * Liebermann reagent * Mandelin reagent * Marquis reagent * Mecke reagent * Pill testing * Simon's reagent * Sullivan reaction The Sullivan reaction is a chemical test used for detecting the presence of cysteine or cystine in proteins. A red colour appears when a protein with cysteine or cystine is heated with sodium 1,2-naphthoquinone-4-sulfonate ( Folin's reagent) and so ... * Zwikker reagent References {{reflis ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sodium Dithionite
Sodium dithionite (also known as sodium hydrosulfite) is a white crystalline powder with a sulfurous odor. Although it is stable in dry air, it decomposes in hot water and in acid solutions. Structure left, 220px, Packing of sodium dithionite ions in a crystal, showing the saw-horse geometry of the dianion. Color code: red = O, yellow = S. The structure has been examined by Raman spectroscopy and X-ray crystallography. The dithionite dianion has C symmetry, with almost eclipsed with a 16° O-S-S-O torsional angle. In the dihydrated form (), the dithionite anion has gauche 56° O-S-S-O torsional angle. A weak S-S bond is indicated by the S-S distance of 239 pm, which is elongated by ca. 30 pm relative to a typical S-S bond. Because this bond is fragile, the dithionite anion dissociates in solution into the O2sup>− radicals, as has been confirmed by EPR spectroscopy. It is also observed that 35S undergoes rapid exchange between S2O42− and SO2 in neutral or acidic solu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Methods
Protein methods are the techniques used to study proteins. There are experimental methods for studying proteins (e.g., for detecting proteins, for isolating and purifying proteins, and for characterizing the structure and function of proteins, often requiring that the protein first be purified). Computational methods typically use computer programs to analyze proteins. However, many experimental methods (e.g., mass spectrometry) require computational analysis of the raw data. Genetic methods Experimental analysis of proteins typically requires expression and purification of proteins. Expression is achieved by manipulating DNA that encodes the protein(s) of interest. Hence, protein analysis usually requires DNA methods, especially cloning. Some examples of genetic methods include conceptual translation, Site-directed mutagenesis, using a fusion protein, and matching allele with disease states. Some proteins have never been directly sequenced, however by translating codons from known ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
