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.
Bar-Zvi, D.; Shavit, N., 1984: Photo affinity labeling of soluble chloroplast atpase with 3 o 4 benzoyl benzoyl adp. Biochimica et Biophysica Acta 765(3): 340-346 3′-O-(4-benzoyl)benzoyl Adp (BzADP) acts as a reversible inhibitor of the chloroplast coupling factor 1 ATPase (Cf1) when incubated with the enyzme in the dark. The Vmax of Atp hydrolysis is [...]
Motoyama, N.; Takimoto, K.; Okada, M.; Nakagawa, H., 1987: Phosphotyrosine phosphatase a novel phosphatase specific for phosphotyrosine 2 amp and p nitrophenylphosphate in rat brain. Journal of Biochemistry (Tokyo) 101(4): 939-948 A unique phosphatase that selectively hydrolyzed phosphotyrosine and 2′-Amp at alkaline pH and – at neutral pH was isolated from a cytosolic fraction of [...]
Fournier P., 1983: Phosphorylated proteins from rat intestinal micro villi membranes electrophoretic similarities with alkaline phosphatase. Molecular Physiology: 323-330 Microvillus membrane, from adult rat small intestine was phosphorylated from Atp. The reaction mixture was studied by Sds-polyacrylamide gel electrophoresis. At the higher Atp concentration utilized, 3 bands of radioactivity could be detected in the phosphorylated [...]
Dimauro S., 1979: Phosphorylase iso enzymes in normal and myo phosphorylase deficient human heart. Neurology: 1538-1541 Phosphorylase isoenzymes were studied by acrylamide-slab electrophoresis in normal tissues and in the heart of a child with a fatal infantile form of myophosphorylase deficiency. Of the 3 bands present in normal human heart, 2 were missing in the [...]
Wunderlich I., 1981: Phosphoryl group transfer by a fraction of the soluble proteins of catecholamine storage vesicles. Journal Of Neurochemistry: 1879-1892 The terminal phosphate group of Atp was transferred to Adp by an enzyme present in the soluble core proteins of bovine adrenal medulla catecholamine storage vesicles. It was purified 10- to 30-fold by Deae [...]
Komkova A.I., 1985: Phosphoprotein phosphatase from bovine spleen cell nuclei physicochemical properties. Biokhimiya: 1067-1075 The physico-chemical properties of phosphoprotein phosphatase (Ec 126.96.36.199) from bovine spleen cell nuclei were investigated. The enzyme was shown to possess a wide substrate specificity and to catalyze dephosphorylation of phosphocasein, Atp, Adp and – (pNPP). The Km values for Atp, [...]
Garlo A.M., 1985: Phosphoglucomutase and esterase d activity in post coital vaginal swabs. Journal Of The Forensic Science Society: 301-312 The study was designed to test the hypothesis that sexual intercourse causes an increase in the activity of vaginal Pgm Semen-free, post-coital vaginal swabs taken at timed intervals were examined, as were swabs taken post [...]
Ooi C.S., 1985: Phosphoglucomutase and glucose phosphate isomerase polymorphism in the mosquito vector anopheles balabacensis from sabah malaysia. Tropical Biomedicine: 185-186 A sample of Anopheles balabacensis derived from eggs collected in Kuala Penyu, Sabah, Malaysia was studied for enzyme variation by means of horizontal starch-gel electrophoresis. Two gene-enzyme systems – phosphoglucomutase and glucose phosphate isomerase [...]
Ratledge C., 1984: Phosphofructokinase and the regulation of the flux of carbon from glucose to lipid in the oleaginous yeast rhodosporidium toruloides. Journal Of General Microbiology2: 3251-3264 Changes in cell composition of R. toruloides Cbs 14 were monitored during growth of batch cultures with NH4Cl and glutamate as N sources. Carbohydrate was synthesized at the [...]
Peterson, J. B.; Evans, H. J., 1979: Phosphoenol pyruvate carboxylase ec 188.8.131.52 from soybean nodule cytosol evidence for iso enzymes and kinetics of the most active component. Biochimica et Biophysica Acta 567(2): 445-452 Phosphoenolpyruvate carboxylase (orthophosphate:oxaloacetate carboxylyase (phosphorylating), Ec 184.108.40.206) from plant cells of soybean nodules was studied to assess its role in providing carbon [...]