Isoenzymes Information and Courses from MediaLab, Inc.
These are the MediaLab courses that cover Isoenzymes and links to relevant pages within the course.
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| All of the following are sources of serum alkaline phosphatase except: | View Page |
| Increases in LD fractions 4 and 5 are indicative of: | View Page |
| Isoenzymes of CK include all of the following except: | View Page |
| Label the scan with CK isoenzyme fractions: | View Page |
| Agarose Gel Agarose gels are chemically purified forms of agar, a polysaccharide extracted from seaweed. The gel pores allow for separation of proteins based on their individual charge and mass. Agarose gel will naturally clear after drying the separated proteins.Common clinical uses of agarose gel electrophoresis (AGE) are separations of plasma proteins, hemoglobin variants, lipoproteins, and isoenzymes. The gels come prepackaged with a plastic template to lay over gel for sample application or slots etched in the gel for these samples. | View Page |
| Routine Electrophoresis Routine electrophoresis is a generic term for the traditional clinical laboratory electrophoresis performed on a rectangle-shaped slab gel. Routine electrophoresis is mostly used for separation of proteins and has some use in separating nucleic acids. Generally several patient specimens and control(s) can be placed on one gel and solutes separated in one run. This type of electrophoresis is sometimes called zone electrophoresis.A serum sample with normal plasma proteins yields five zones or bands of separated proteins: albumin, alpha-1-globulins, alpha-2-globulins, beta-globulins, and gamma-globulins. Proteins in CSF and urine proteins are also separated with routine electrophoresis. Using whole blood treated with a reagent to lyse red blood cells, variant and glycosylated hemoglobins can be detected. With different visualization methods, isoenzymes and lipoproteins in a serum sample can be identified.A manual agarose gel electrophoresis of eight serum samples is pictured below. After electrophoresis, the gel was stained with Ponceau S. | View Page |
| IEF Advantages and Applications IEF's greatest advantage is its high resolution, resulting in greater separation of solutes. IEF of serum proteins results in many more bands; these bands are sharper because each pH region is very narrow. Performing IEF is easier because the placement of sample application is not important. The sample and ampholytes can be mixed before application; the ampholytes will migrate, create the gradient, and then the proteins separate and migrate.Some isoenzymes and variant hemoglobins in prenatal screening are separated with IEF. Detection of oligoclonal bands in gamma-globulin is a newer use of IEF. IEF is commonly used as one of the separations in two-dimensional electrophoresis. | View Page |