Abstract
Addition of small amphoteric substances or separators to the carrier ampholytes used in isoelectric focusing improves the separation of protein components. The technique has been applied to partially oxidized human hemoglobin, goat anti-bovine pancreatic oxidized ribonuclease, human γ-globulin, and barley β-amylase. Each of these proteins is a complex mixture of species which can be resolved selectively and reproducibly by this method. Superior separation is provided by this technique when compared to focusing in commercially available narrow-range ampholytes. Addition of separators usually results in the flattening of the pH profile of the gel. Inspection of the protein patterns indicates that no new protein bands arise, although different patterns of existing components are obtained by choice and concentration of separator as well as by concentration of carrier ampholytes. This technique, thus, offers the advantage of making conventional isoelectric focusing more versatile.
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