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.
Kato H., 1987: Precipitate forming reaction of beta 1 4 d glucanase i in malt. Agricultural & Biological Chemistry: 655-664 Beta.-(1.fwdarw.4)-D-glucanase (1) was isolated and purified to homogeneity by Sds-gel electrophoresis from brewing malt. The enzyme had an endo-hydrolase action pattern against.beta.-glucan and carboxymethyl cellulose, while it formed precipitates having mainly linear.beta.-(1.fwdarw.4) linkages in the [...]
Kato H., 1986: Precipitate forming reaction of beta 1 4 d glucanase ii in malt. Agricultural & Biological Chemistry: 733-740 Beta.-(1.fwdarw. 4)-D-Glucanase was isolated and purified to homogeneity on Sds-electrophoresis from brewing barley malt. This enzyme had an endo-hydrolase action pattern on.beta.-glucan prepared from the same malt, while the enzyme formed precipitates in the reaction [...]
Carp, H.; Miller, F.; Hoidal, J. R.; Janoff, A., 1982: Potential mechanism of emphysema alpha 1 proteinase inhibitor recovered from lungs of cigarette smokers contains oxidized methionine and has decreased elastase ec 18.104.22.168 inhibitory capacity. Proceedings of the National Academy of Sciences of the United States of America 79(6): 2041-2045 The elastase inhibitory capacity per [...]
Robertson, L. W.; Parkinson, A.; Bandiera, S.; Safe, S., 1981: Potent induction of rat liver microsomal drug metabolizing enzymes by 2 3 3 4 4 5 hexa bromo bi phenyl a component of firemaster. Chemico Biological Interactions 35(1): 13-24 The multistep synthesis and purification of 2,3,3′,4,4′,5-hexabromobiphenyl (HBBp) is described. Capillary gas chromatography revealed that HBBp [...]
Schrijen, J. J.; Van-Groningen-Luyben, W. A. H. M.; Nauta, H.; De-Pont, J. J. H. H. M.; Bonting, S. L., 1983: Potassium proton atpase determination of the molecular size by radiation inactivation analysis. Biochimica et Biophysica Acta 731(2): 329-337 A (K++H+)-ATPase containing membrane fraction, isolated from pig gastric mucosa, was further purified by zonal electrophoresis, leading [...]
Ingoglia N.A., 1987: Posttranslational protein modification by polyamines in intact and regenerating nerves. Journal Of Neurochemistry: 669-675 A 150,000-g supernatant from axoplasm of the giant axon of the stellate nerve of the squid and from rat sciatic and goldfish optic nerves was found to be able to incorporate covalently putrescine and spermidine into an exogenous [...]
Siegel F.L., 1986: Posttranslational modification of calmodulin in rat brain and pituitary. Journal Of Neurochemistry: 164-172 The posttranslational modification of calmodulin has been studied in six brain regions and the anterior pituitary. Carboxylmethylation, calmodulin converting enzyme, and calmodulin (lysine) N-methyltransferase activities were determined. Incubation of calmodulin with cytosolic extracts of these tissues in the presence [...]
Conboy, J. G.; Rosenberg, L. E., 1981: Post translational uptake and processing of in vitro synthesized ornithine trans carbamoylase ec 22.214.171.124 precursor by isolated rat liver mitochondria. Proceedings of the National Academy of Sciences of the United States of America 78(5): 3073-3077 The mitochondrial matrix enzyme ornithine transcarbamoylase (OTCase; ornithine carbamoyltransferase; carbamoylphosphate:L-ornithine carbamoyltransferase, Ec 126.96.36.199) [...]
Bischoff, D.; Luppa, H.; Andra, J., 1982: Post natal development of acetyl cholin esterase ec 188.8.131.52 in selected rat brain regions behavior of its multiple forms in the medial septal nucleus and hippocampus. Acta Histochemica et Cytochemica 15(6): 807-811 The behavior of the multiple forms of soluble and Triton-solubilized acetylcholinesterase was investigated using microgel gradient [...]
Sun S.H., 1988: Possible role of a proteinase in endosporulation of coccidioides immitis. Infection & Immunity: 1551-1559 We previously reported isolation of a serine proteinase from the soluble conidial wall fraction of Coccidioides immitis. The purified proteinase was identified as a polypeptide band of 36,000 Mr by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In this study, [...]