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|Title:||Serum and urine electrophoresis for detection and identification of monoclonal proteins.|
|Authors:||Jenkins, Margaret A|
|Affiliation:||Austin Health, Heidelberg, Vic 3084, Australia|
|Citation:||The Clinical Biochemist. Reviews / Australian Association of Clinical Biochemists; 30(3): 119-22|
|Abstract:||Electrophoresis may be defined as the separation of charged particles in a uniform electric field. For a particular system of electrophoresis, the voltage is held constant as are the pH and ionic strength of the suspending medium. Tiselius, using a moving boundary liquid system, separated serum proteins by electrophoresis into four components in 1937. Paper electrophoresis, popular in the 1950s, provided the rst solid electrophoresis support. The fragility of paper as a support medium saw the introduction of the more robust cellulose acetate a decade later. An improvement in resolution was subsequently gained by using agarose gel, which, in serum samples, gave 5 bands of separation. In the late 1980s, high resolution agarose gels were introduced which produced at least 6 bands, and depending on the system, as many as 17 bands in serum. Fully automated serum electrophoresis commenced in the 1990s with the introduction of capillary electrophoresis (CE), a reintroduction of a liquid medium but with exquisite resolution compared to Tiselius' procedure. Using CE instrumentation it is possible to program a sequence of samples and leave them overnight to be processed.Amalgamation of laboratories with an increasing number of patient samples was probably the reason for the semi-automation of gel electrophoresis. The introduction of the Helena SPIFE and Sebia Hydrasys gel systems provided ways of electrophoresing over a hundred serum samples per day. There is certainly a role for such instrumentation in electrophoresis laboratories today.|
|Internal ID Number:||19841694|
|Appears in Collections:||Journal articles|
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