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- W1441507961 abstract "Remarkable progress in the techniques of molecular biology has advanced the field of protein sequencing immeasurably. A highly specific isolation method, such as affinity chromatography is essential to the success of such an undertaking. The nonspecific attachment of peptide hormones to activated Sepharose resins can generate a number of different species with varying affinities for the desired receptor. There are a number of advantages to the avidin–biotin technique. The formation of affinity column is highly specific—namely, through the avidin–biotin interaction and is achieved by simply mixing the biotinylated ligand with the Sepharose-immobilized suc-avidin resin. Avidin is a highly basic glycoprotein composed of four identical subunits, each having a biotin-binding site. The use of this protein for the construction of affinity columns has the serious disadvantage that avidin binds nonspecifically to many components, especially negatively charged membrane proteins. This property can be eliminated by exhaustively succinoylating avidin with succinic anhydride to form suc-avidin." @default.
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- W1441507961 date "1990-01-01" @default.
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- W1441507961 title "[27] Isolation and characterization of hormone receptors" @default.
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- W1441507961 doi "https://doi.org/10.1016/0076-6879(90)84281-k" @default.
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