The xanthoproteic reaction is a method that can be used to detect a presence of protein soluble in a solution, using concentrated nitric acid. The test gives a positive result in amino acids carrying aromatic groups, especially in the presence of tyrosine. If the test is positive the proof is neutralized with an alkali, turning dark yellow. The yellow colour is due to xanthoproteic acid which is formed due to nitration of certain amino acids, most common examples being tyrosine and tryptophan. [1] This chemical reaction is a qualitative test, determining the presence or absence of proteins.
Add 1 ml of concentrated HNO3 to 1 ml of the test sample. Gently heat the mixture and cool it. Slowly add sodium hydroxide (NaOH, 40 % w/v in water) solution until the mixture becomes alkaline and a colour change is observed. If the colour changes from yellow to orange, this indicates the presence of an aromatic amino acid.
When human skin or nails are exposed to nitric acid, they turn yellow after some time, indicating the presence of protein. The finger nails show a bright yellow colour (finger nails are made up of keratin, which is a protein) which cannot be scraped off, unlike the yellow colouration on the skin, which can be peeled off.[ citation needed ]
Nitric acid is the inorganic compound with the formula HNO3. It is a highly corrosive mineral acid. The compound is colorless, but samples tend to acquire a yellow cast over time due to decomposition into oxides of nitrogen. Most commercially available nitric acid has a concentration of 68% in water. When the solution contains more than 86% HNO3, it is referred to as fuming nitric acid. Depending on the amount of nitrogen dioxide present, fuming nitric acid is further characterized as red fuming nitric acid at concentrations above 86%, or white fuming nitric acid at concentrations above 95%.
Protein primary structure is the linear sequence of amino acids in a peptide or protein. By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the laboratory. Protein primary structures can be directly sequenced, or inferred from DNA sequences.
Urea, also called carbamide, is an organic compound with chemical formula CO(NH2)2. This amide has two amino groups joined by a carbonyl functional group. It is thus the simplest amide of carbamic acid.
Phenylalanine is an essential α-amino acid with the formula C
9H
11NO
2. It can be viewed as a benzyl group substituted for the methyl group of alanine, or a phenyl group in place of a terminal hydrogen of alanine. This essential amino acid is classified as neutral, and nonpolar because of the inert and hydrophobic nature of the benzyl side chain. The L-isomer is used to biochemically form proteins coded for by DNA. Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the biological pigment melanin. It is encoded by the messenger RNA codons UUU and UUC.
An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized from scratch by the organism fast enough to supply its demand, and must therefore come from the diet. Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are valine, isoleucine, leucine, methionine, phenylalanine, tryptophan, threonine, histidine, and lysine.
In organic chemistry, nitration is a general class of chemical processes for the introduction of a nitro group into an organic compound. The term also is applied incorrectly to the different process of forming nitrate esters between alcohols and nitric acid. The difference between the resulting molecular structures of nitro compounds and nitrates is that the nitrogen atom in nitro compounds is directly bonded to a non-oxygen atom, whereas in nitrate esters, the nitrogen is bonded to an oxygen atom that in turn usually is bonded to a carbon atom.
Potassium dichromate, K2Cr2O7, is a common inorganic chemical reagent, most commonly used as an oxidizing agent in various laboratory and industrial applications. As with all hexavalent chromium compounds, it is acutely and chronically harmful to health. It is a crystalline ionic solid with a very bright, red-orange color. The salt is popular in laboratories because it is not deliquescent, in contrast to the more industrially relevant salt sodium dichromate.
Classical qualitative inorganic analysis is a method of analytical chemistry which seeks to find the elemental composition of inorganic compounds. It is mainly focused on detecting ions in an aqueous solution, therefore materials in other forms may need to be brought to this state before using standard methods. The solution is then treated with various reagents to test for reactions characteristic of certain ions, which may cause color change, precipitation and other visible changes.
In chemistry, the Biuret test, also known as Piotrowski's test, is a chemical test used for detecting the presence of at least two peptide bonds in a molecule. In the presence of peptides, a copper(II) ion forms mauve-colored coordination complexes in an alkaline solution. The reaction was first observed in 1833; In Poland, the biuret test is also known as Piotrowski's test in honor of the Polish physiologist Gustaw Piotrowski who independently rediscovered it in 1857. Several variants on the test have been developed, such as the BCA test and the Modified Lowry test.
An aromatic amino acid is an amino acid that includes an aromatic ring.
A range of qualitative and quantitative tests have been developed to detect phosphate ions (PO43-) in solution. Such tests find use in industrial processes, scientific research, and environmental water monitoring.
Millon's reagent is an analytical reagent used to detect the presence of soluble proteins. A few drops of the reagent are added to the test solution, which is then heated gently. A reddish-brown coloration or precipitate indicates the presence of tyrosine residue which occur in nearly all proteins. The test was developed by the French chemist Auguste Nicolas Eugene Millon.
A urine test strip or dipstick is a basic diagnostic tool used to determine pathological changes in a patient's urine in standard urinalysis.
The Trinder spot test is a diagnostic test used in medicine to determine exposure to salicylates, particularly to salicylic acid. The test employs the Trinder reagent which is mixed with a patient's urine. The colour change, resulting from the Trinder reaction, is immediate, enabling rapid bedside assessment.
In physical and analytical chemistry, colorimetry or colourimetry is a technique used to determine the concentration of colored compounds in solution. A colorimeter is a device used to test the magnitude of a solution by measuring its absorbance of a specific wavelength of light.
Certain diseases can cause excessive accumulations of fluid in areas of the body such as the abdomen (ascites) or the pleural space around the lungs or the pericardial space around the heart. An estimate of the concentration of protein in such fluids can narrow the differential diagnosis and assist the clinician in establishing a diagnosis. For example, fluid accumulations due to congestive heart failure and liver failure (cirrhosis) are typically lower in protein content and are called transudates whereas fluid accumulations due to cancer and tuberculosis are typically higher in protein content and are called exudates. The Rivalta Test is a simple, inexpensive method that can be used in resource-limited settings to differentiate a transudate from an exudate. It is a simple, inexpensive method that does not require special laboratory equipment and can be easily performed in private practice. The test was originally developed by the Italian researcher Rivalta around 1900 and was used to differentiate transudates and exudates in human patients. It is also useful in cats to differentiate between effusions due to feline infectious peritonitis (FIP) and effusions caused by other diseases. Not only the high protein content, but high concentrations of fibrinogen and inflammatory mediators lead to a positive reaction.
Xanthoproteic acid is a non-crystallizable yellow substance derived from proteins upon treatment with nitric acid. Nitric acid reacts with proteins to form xanthoproteic acid. This reaction is known as the xanthoproteic reaction. This test is carried out by adding concentrated nitric acid to the substance being tested, and then heating the mixture. If proteins are present that contains amino acids with aromatic rings, the mixture turns yellow. Upon adding a strong base, such as ammonia solution, the color turns orange. These color changes are caused by nitrated aromatic rings in the protein. The xanthoproteic test is specific for aromatic compounds such as tyrosine, tryptophan and phenylalanine.
The Denigés' reagent is a reagent used for qualitative analysis. It was developed in 1898 by Georges Denigés, a French biochemist.
A spot test in lichenology is a spot analysis used to help identify lichens. It is performed by placing a drop of a chemical reagent on different parts of the lichen and noting the colour change associated with application of the chemical. The tests are routinely encountered in dichotomous keys for lichen species, and they take advantage of the wide array of lichen products produced by lichens and their uniqueness among taxa. As such, spot tests reveal the presence or absence of chemicals in various parts of a lichen. They were first proposed as a method to help identify species by the Finnish lichenologist William Nylander in 1866.
Salkowski's test, also known simply as Salkowski test, is a qualitative chemical test, that is used in chemistry and biochemistry for detecting a presence of cholesterol and other sterols. This biochemical method got its name after German biochemist Ernst Leopold Salkowski, who is known for development of multiple new chemical tests, that are used for detection of different kinds of molecules. A solution that has tested positive on the Salkowski's test becomes red and gets yellow glow.