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Phosphopeptide enrichment is the process of isolating phosphorylated proteins from tissues and cells. Isolating phosphopeptides is difficult because protein phosphorylation is transient, phosphate groups can fall off during purification, phosphopeptides may be be produced at low levels, and phospho-specific antibodies for affinity purification perform poorly. The general purification steps for phosphopeptides are the same as other proteins: 1) extraction of proteins through cell lysis, 2) precipitation of all proteins in a salt buffer, 3) collection of the precipitated proteins through ultracentrifugation, 4) purification of the desired protein, 5) removal of residual salts, and 6) refolding, if the proteins are denatured (unfolded) during purification. Additional steps for phosphopeptide purification include the inhibition of phosphatases and often the denaturation of proteins to expose phosphate groups. For enrichment, chromatography techniques that exploit the phosphate group are usually employed and include ion exchange, immobilized metal affinity chromatography (IMAC), and hydroxyapatite chromatography. Phosphopeptide enrichment can be used to study cellular signal transduction, cell cycle control in cancer cells, and stem cell differentiation. (Credit: Brooke Anderson-White)
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