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Gel extraction kits are available from several major biotech manufacturers for a final cost of approximately 1–2 US$ per sample. Protocols included in these kits generally call for the dissolution of the gel-slice in 3 volumes of chaotropic agent at 50 °C, followed by application of the solution to a spin-column (the DNA remains in the column), a 70% ethanol wash (the DNA remains in the ...
Allantoin is a major metabolic intermediate in most organisms including animals, plants and bacteria, though not humans. It is produced from uric acid, which itself is a degradation product of nucleic acids, by action of urate oxidase (uricase). [3] [4] [5] Allantoin also occurs as a natural mineral compound (IMA symbol Aan [6]).
Elution principle of column chromatography. In analytical and organic chemistry, elution is the process of extracting one material from another by washing with a solvent: washing of loaded ion-exchange resins to remove captured ions, or eluting proteins or other biopolymers from a gel electrophoresis or chromatography column.
Electroelution is a method used to extract a nucleic acid or a protein sample from an electrophoresis gel by applying a negative current in the plane of the smallest dimension of the gel, drawing the macromolecule to the surface for extraction and subsequent analysis. [2]
During electrophoresis in a discontinuous gel system, an ion gradient is formed in the early stage of electrophoresis that causes all of the proteins to focus into a single sharp band. The formation of the ion gradient is achieved by choosing a pH value at which the ions of the buffer are only moderately charged compared to the SDS-coated proteins.
TAE buffer is commonly prepared as a 50× stock solution for laboratory use. A 50× stock solution can be prepared by dissolving 242 g Tris base in water, adding 57.1 ml glacial acetic acid, and 100 ml of 500 mM EDTA (pH 8.0) solution, and bringing the final volume up to 1 litre.
Salt compounds dissociate in aqueous solutions. This property is exploited in the process of salting out. When the salt concentration is increased, some of the water molecules are attracted by the salt ions, which decreases the number of water molecules available to interact with the charged part of the protein. [3]
The drying of the gel does not seem to support the process. [7] [16] Therefore, the improvement of the in-gel digestion has to be achieved by the reduction of the way of the enzyme to its substrate e.g. by cutting the gel to pieces as small as possible. Usually, the in-gel digestion is run as an overnight process.
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