Gel Electrophoresis

The separation of polypeptides by electrophoresis allowed Arne Tiselius to describe protein fractions corresponding to albumin, -, -, and -globulins in serum with the Rrst published diagram of human serum protein electrophoresis in 1939. The number of fractions slowly expanded into electrophoretic subfractions identiRed as 1, 2, 1, 2, 1 and 2. The mobility characteristics of these fractions are still used to denote serum proteins such as 1macroglobulin, 2-antiplasmin or 2-microglobulin. Sophisticated new electrophoretic techniques for identifying many proteins simultaneously and relating them to diseases have been developed over the years, many of them being described in other studies. Almost all body Suids have been studied by electrophoresis, serum, urine and cerebrospinal Suid being evaluated in great detail by different techniques. However, despite the major developments and progress achieved in protein separation, only a restricted number of methods are routinely used in the clinical laboratory. Nowadays, serum protein electrophoresis is mainly used to study major serum protein alterations such as those observed in patients with inSammatory, liver or kidney diseases, as well as in patients presenting lymphoproliferative disorders and alterations of immunoglobulin (Ig) production. Electrophoretic techniques, in association with ultracentrifugation, are also used to study lipoproteins and to classify hyperlipidaemic disorders. Here, we provide selected clinical situations studied by electrophoretic methods, with a particular emphasis on 2D-PAGE, in order to illustrate how electrophoresis can be used to gain insight into particular clinical problems.