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containing a distribution of pore sizes. Larger molecules are excluded from the pores, and hence run through the column quickly, whereas smaller and smaller molecules have to navigate smaller and smaller pores, resulting in separation according to molecular weight. The range of separation depends on the pore size; certain pore sizes are best for separating in the small biomolecule range (>10 kDa), through to large analytes such as proteins (<200 kDa) and even up to the mass of small plasmids, organelles or viruses. This method is the softest separation technique, since analytes are never actually changing their physical environment, nor actually binding to resin during the chromatography. GFC is often used as a nal polishing step in a puri cation procedure. One certain special class of gel ltration chromatography columns are known as desalting columns (or buffer exchange columns). A resin is used that completely excludes large analytes, but has no exclusion for salt, solvent or buffer molecules. The column is rst equilibrated in the desired buffer that the analyte is to be transferred to, then a sample of analyte is applied, to elute well before the sample salts and buffers that otherwise get caught in the pores of the column. For small volumes, this technique tends to be quicker than dialysis, and is often useful for unstable molecules where dialysis would take too long. GFC even enables researchers to get a handle on the quaternary structure of proteins, as the columns may be calibrated with known proteins, and an approximate mass directly estimated from the time of elution. asp.net code 128 reader C# Code 128 Reader SDK to read, scan Code 128 in C#.NET class ...
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