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2. Illustration of electrophoresis retardation. Electrophoresis is the motion of charged dispersed particles or dissolved charged molecules relative to a fluid under the influence of a spatially uniform electric field. As a rule, these are zwitterions. [1] Electrophoresis is used in laboratories to separate macromolecules based on their
Serum protein electrophoresis (SPEP or SPE) is a laboratory test that examines specific proteins in the blood called globulins. [1] The most common indications for a serum protein electrophoresis test are to diagnose or monitor multiple myeloma , a monoclonal gammopathy of uncertain significance (MGUS), or further investigate a discrepancy ...
The test uses the principles of gel electrophoresis to separate out the various types of hemoglobin and is a type of native gel electrophoresis.After the sample has been treated to release the hemoglobin from the red cells, it is introduced into a porous gel (usually made of agarose or cellulose acetate) and subjected to an electrical field, most commonly in an alkaline medium.
In medicine, protein electrophoresis is a method of analysing the proteins mainly in blood serum. Before the widespread use of gel electrophoresis , protein electrophoresis was performed as free-flow electrophoresis (on paper) or as immunoelectrophoresis.
Counter-immunoelectrophoresis and its modification. In comparison to other conventional methods of diagnosis e.g. for viral infection testing, counter-immunoelectrophoresis is a highly specific, simple, and speedy method that does not require sophisticated, expensive tools, input materials, or long-term capacity building.
A disease of gamma globulins is called a "gammopathy" (for example, in monoclonal gammopathy of undetermined significance). Brutton's agammaglobulinemia is an X-linked recessive disorder characterized by recurrent infections in the early-post natal period attributable to failure of pre-B cells to mature.
Proteins of the erythrocyte membrane separated by SDS-PAGE according to their molecular masses. SDS-PAGE (sodium dodecyl sulfate–polyacrylamide gel electrophoresis) is a discontinuous electrophoretic system developed by Ulrich K. Laemmli which is commonly used as a method to separate proteins with molecular masses between 5 and 250 kDa.
Pipetting anti-immunoglobulins to immunofixation panel. The panel simultaneously tests 4 patients (one in each quadrant). Each patient has 6 electrophoresis panels: The left one is a conventional serum protein electrophoresis. The remainder get solutions with anti-IgG, anti-IgA, anti-IgM, anti-kappa light chain and anti-lambda light chain ...