In the field of biochemistry, there are two types of electrophoresis: the nucleic acid electrophoresis and the electrophoresis of proteins.
Nucleic acid electrophoresis, or DNA electrophoresis, is an analytical technique that allows a scientist or researcher to separate DNA or RNA fragments according to their size and reactivity. The nucleic acids that are to be analyzed using this process are set upon a gel medium, where an electric field will be used to induce the nucleic acids toward the anode. This is made possible by the net negative charge of the backbone of the nucleic acid chain, which is made of sugar and phosphate molecules. The separation of the nucleic acid fragments is done through exploiting the mobilities, with which molecules of different sizes are able to pass through the viscous medium. Smaller fragments typically end up nearer to the anode, while longer molecules migrate more slowly because the gel provides resistance to these particles. After a certain amount of time, the electric current will be removed and the resulting fragmentation gradient is analyzed.
Protein electrophoresis, on the other hand, uses a fluid or an extract in order to analyze the proteins contained within. Typically, a protein electrophoresis is performed with a small amount of the sample used in alternative ways—either with or without a supporting medium. There are different kinds of protein electrophoresis, including SDS polyacrylamide gel electrophoresis, electrofocusing, free flow electrophoresis, isotachophoresis, affinity electrophoresis, immunoelectrophoresis, counterelectrophoresis, and capillary electrophoresis. Each of these methods has different variations, as well as individual advantages and limitations. However, protein electrophoresis is limited by practical limitations regarding its use as a preparative method. Protein electrophoresis is very useful in medicine in terms of analyzing the proteins present in the blood serum.
This category contains scientific information on electrophoresis, a process used in biochemistry to determine and evaluate proteins or enzymes within a specific sample.
Battersby, R.; Holloway, C. J., 1982: Preparative isotachophoresis in a flat bed of granulated gel principles and procedures comparison with iso electric focusing and application to the isolation of a low iso electric point high mobility form of cat liver cytosolic glutathione s transferase ec 18.104.22.168. Electrophoresis 3(5): 275-284 A method is reported for the [...]
Hansson C., 1983: Preparative affinity electrophoresis application to human erythrocyte carbonic anhydrase. Analytical Biochemistry: 259-263 The modification of affinity electrophoresis for preparative purposes is described. This method was applied to the purification of human erythrocyte carbonic anhydrases B and C. During conventional affinity chromatography some Hb contamination occurs. By introduction of an electrophoretic purification step [...]
Schroeter D., 1986: Preparation of two plasma membrane fractions from ascites tumor cells by gel chromatography on sephacryl s 1000. Journal Of Chromatography Biomedical Applications: 07-116 Two plasma membrane fractions from ascites tumour cells with differences in vesicle size were isolated by gel-exclusion chromatography on Sephacryl S-1000. Fraction 1 appeared in the void volume and [...]
Wood, T., 1981: Preparation of transketolase ec 22.214.171.124 free from d ribulose 5 phosphate 3 epimerase ec 126.96.36.199. Biochimica et Biophysica Acta 659(2): 233-243 A procedure for the purification from Candida utilis of transketolase (sedoheptulose-7-phosphate: D-glyceraldehyde-3-phosphate glycolaldehydetransferase, Ec 188.8.131.52) free from D-ribulose-5-phosphate 3-epimerase (Ec 184.108.40.206) was developed using acetone precipitation, elution from Deae-cellulose, adsorption of [...]
Lee K Y., 1985: Preparation of restriction endonuclease alu i from arthrobacter luteus. Korean Journal Of Biochemistry: 149-154 Extraction and purification of the restriction endonuclease, Alu-I, were performed from Arthrobacter luteus. The harvested cells were disrupted by the treatment of lysozyme and sonification, and the supernatant was precipitated with 70% saturation of ammonium sulfate. The [...]
Su J C., 1985: Preparation of pancreatin and purification of lipase from hog pancreas. Proceedings Of The National Science Council Re Ic Of China Part B Life Sciences: 75-81 Pancreatin containing high activities of proteolytic enzymes, amylase and lipase was prepared from optimally autolyzed hog pancreas. About 100 g of pancreatin were obtained from 1 [...]
Gehrke L., 1986: Preparation of messenger rna transcripts for secondary structure analysis using sp 6 polymerase guanylyltransferase and preparative gel electrophoresis. Gene Analysis Techniques: 45-52 Undegraded radiolabeled messenger Rna (mRNA) is required for the experimental analysis of mRNA secondary structure. The introduction of plasmids containing the Sp6 promoter allows the in vitro synthesis of relatively [...]
Wells W.W., 1987: Preparation of homogeneous pig liver thioltransferase by a thiol disulfide mediated pi shift. Analytical Biochemistry: 265-273 An enzyme catalyzing thiol-disulfide exchange, thioltransferase, was purified to homogeneity from pig liver. By taking advantage of the relatively large pI shift of the enzyme between its reduced and disulfide forms, the purification procedure, which included [...]
Barath Z., 1983: Preparation of highly purified mitochondria of neurospora crassa on a percoll gradient. Folia Microbiologica: 409-413 Mitochondria isolated from N. crassa were purified by centrifugation in a Percoll density gradient. Enzyme activities and cytochrome differential spectra revealed high purity of the mitochondria. As compared with a crude mitochondrial fraction the purified mitochondria exhibited [...]
Smith, D. J.; Taubman, M. A.; Ebersole, J. L., 1979: Preparation of glucosyl transferase ec 220.127.116.11 from streptococcus mutans by evolution from water insoluble poly saccharide with a dissociating solvent. Infection and Immunity 23(2): 446-452 Glucosyltransferase (Ec 18.104.22.168) was obtained by dissociation from water-insoluble polysaccharide in the presence of 6 M guanidine-hydrochloride. Water-insoluble polysaccharide was [...]