Electrophoretic pattern of proteins

Gel Electrophoresis. Electrophoretic patterns of proteins in untreated and enzymatically hydrolyzed peanut flour showed that the proteins of pepsin and bromelain controls were markedly different from those of nontreated flour (Figure 14). Heating these two controls under acidic conditions not only decreased protein solubility, but also changed the proteins qualitatively. 

Electrophoretic pattern of proteins Protein pattern of mutants and parent strains was analysed by polyacrylamide gel electrophoresis (PAGE) using the method of Davis(22). 

Electrophoretic protein pattern The electrophoretic pattern of protein (Table III) revealed extra bands in two of the edifenphos-resistant mutants (POLR-1 and POLR-4) of P. oryzae. POLR-2 did not show any extra band. In D. oryzae there was no difference in the number of protein bands but the intensity was greater in all the edifenphos-resistant mutants. 

Figure 7. Electrophoretic patterns of proteins which are released from thyla-koids during freezing or exposure to 0°C in the presence of various solutes. The solute concentration before freezing is indicated under the gels. Freezing time was 3 hours at —25°C. After thawing, supernatant fluids from membranes were treated with sodium dodecylsulfate (SD) and mercaptoethanol then subjected to gel electrophoresis. Phe is sodium phenylpyruvate, Cap is sodium caprylate, lie is isoleucine. From Volger, Heber, and Berzborn (48).

Female apocrine proteins also have been electrophoretically separated and probed with antisera to ASOBl and 2. The electrophoretic pattern of proteins and Western blotting results were qualitatively similar to that for male apocrine proteins (Spielman, et al., 1998). 

Ulrikson, G.U. 1971. Radiation effects on serum proteins, hematocrits, electrophoretic patterns and protein components in the bluegill (Lepomis macrochirus). Pages 1100-1105 in D.J. Nelson (ed.). Radionuclides in Ecosystems. Proceedings of the Third National Symposium on Radioecology. May 10-12, 1971, Oak Ridge, TN. Vol. 1. Available from Natl. Tech. Infor. Serv., Springfield, VA 22151. 

Gel electrophoretic patterns of water-soluble proteins in the five peanut flours were determined as previously described (2) and show considerable differences in protein character (Figure 2). In... 

Figure 2. Typical disc polyacrylamide gel electrophoretic patterns of water-soluble proteins from peanut flours. Reproduced with permission from Ref. 2. Copyright 1980, Institute of Food Technologists.

Separation of a mixture of proteins by electrophoretic techniques such as polyacrylamide gel, SDS polyacrylamide or iso-electric focusing usually results in a complex pattern of protein bands or zones. Interpretation of the results often involves a comparison of the patterns of test and reference mixtures and identification of an individual protein, even using immunoelectrophoresis (Figure 11.15), is very difficult. However, specific proteins can often be identified using an immunoblotting technique known as Western blotting. The prerequisite is the availability of an antibody, either polyclonal or monoclonal, against the test protein. 

Photodynamic treatment equally affects viral particles and protein components in biological fluid, but virions, being large supramolecular structures, are more vulnerable compared to protein molecules. For this reason, damage to one of the components of a virion leads to inactivation of the entire viral particle without affecting the growth properties of semm or the electrophoretic pattern of the proteins. 

An Illustration of the Electrophoretic Pattern of Blood Serum Proteins... 

Figure 11. Polyacrylamide disc gel electrophoretic patterns of extracellular proteins produced by T. reesei QM 9414. The sample applied to the gel on the left was 130 fig extracellular protein from T. reesei my-celia grown on 1% Avicel (29), that applied to the gel on the right was 120 fig extracellular protein produced from sophorose-incubated mycelia. The bands shown here were stained for protein with Coomassie Blue and could, in all cases, also be stained for carbohydrate with the periodic acid-Schiff reagent.

Figure 12. Polyacrylamide disc gel electrophoretic patterns of enzymes purified from the extracellular protein produced by T. reesei QM 9414 in response to ImM sophorose. To the gels, from left to right, were applied 175 fig extracellular protein mixture, 45 fig CBH II, 45 fig endoglucanase and 80 fig CBH I (D).

L Bini, B Magi, B Marzocchi, C Cellesi, B Berti, R Raggiaschi, A Rossolini, V Pallini. Two-dimensional electrophoretic patterns of acute-phase human serum proteins in the course of bacterial and viral diseases. Electrophoresis 17 612-616,1996. 

FA Witzmann, CD Fultz, JC Lipscomb. Toxicant-induced alterations in two-dimensional electrophoretic patterns of hepatic and renal stress proteins. Electrophoresis 17 198-202, 1996. 

Song, S., Singh, A.K., Kirby, B.J., Electrophoretic concentration of proteins at laser-patterned nanoporous membranes in microchips. Anal. Chem. 2004, 76, 4589—4592. 

Fig. 4. Rising electrophoretic patterns of conalbumin obtained after dialysis of a pH 3 solution at pH 5.3 for various lengths of time. The lapse of time between starting the dialysis and electrophoresis of the protein is given under each pattern. The ionic strength in these experiments was 0.16. (Arch. Biochem. Biophys. 52, 48 [1954]).

Fig. 22a-f Photograph of starch gel electrophoretic patterns of avian egg whites to which Fe59 had been added before electrophoresis, a, c, and e are photographs of the gel stained for protein with Amido black, and b, d, and f are the corresponding autoradiograms which indicate the position of the conalbumin in the starch gel. (Clark, J. R., D. T. Osuga, and R. E. Feeney (1963) Comparison of avian egg white conalbumins. (J. Biol. Chem. 238, 3621 [1963])). 

Figure 7.5 Electrophoretic patterns of erythrocyte lysates bearing abnormal hemoglobins. C, A2, S, F, Al7 Barts, and H are hemoglobins C, A2, S (sickle), Aa (normal), Barts and H, respectively. Electrophoresis was done at pH 8.6, the medium was stained with a protein-specific dye, and the bound dye was quantitated densitometrically. Absorbance is on the y axis, distance moved, on the x axis, Shaded areas represent abnormal patterns. (From a circular by Gelman Instrument Co., Ann Arbor, MI, by permission of the copyright holder.)...

Fig. 1. A The electrophoretic pattern of gastric juice from a healthy subject in 0.1 ionic strength veronal buffer at pH 8.6 and a protein concentration of 3.9. B The same after addition of glandular mucoprotein. C The same as A after addition of mucoproteose. From Mack et al. (Ml).

About 350 electrophoretic strips were cut into 0.5-cm segments and after elution were analyzed for proteins, hexoses, hexosamine, fucose, sialic and uronic acids, and sulfates. Results obtained were correlated with the mean electrophoretic pattern of the same gastric juice pool stained by amido black and PAS stains, traced in Analytrol, and analyzed by means of Gaussian curves (Fig. 10). 

Fig. 17. Electrophoretic pattern of neutralized gastric juice on starch block, pH 6.1, 30 hours, 400 volts. The figures indicate regularly occurring protein peaks. From Grasbeck (G27).

Another change in the electrophoretic pattern of gastric juice, as a result of peptic digestion, was the marked decrease in size of the protein component localized about 1 cm toward the anode from the origin. This parallels findings obtained under similar conditions vith other techniques, i.e., decrease or disappearance of component B on starch block electrophoresis (K7), of component M4 on horizontal paper electrophoresis (B13), and of the intermediate tertiary Bia binder on vertical paper electrophoresis (G23, Ul, U2). 

Because CSF is mainly an ultrafiltrate of plasma, low molecular weight plasma proteins such as prealbumin, albumin, and transferrin normally predominate. No protein with a molecular weight greater than that of IgG is present in sufficient concentration to be visible on electrophoresis. The electrophoretic pattern of normal CSF after concentrating the fluid has two striking features—a prominent prealbumin band and two transferrin bands. The second of the electrophoretic transferrin bands is the x (tau) protein band, which is produced or transformed intrathecally and, by comparison with plasma transferrin, is deficient in sialic acid content. 

Schematic representations of sodium dodecyl sulfate polyacrylamide gel electrophoretic patterns of red blood cell membranes (M) and membrane skeletons (S), based on work by Fairbanks and Steck. Proteins are stained with Coomassie blue (CB) and sialoglycoproteins with periodic acid-Schiff (PAS). GPA, GPB, and GPC are glycophorin A. B, and C, respectively G3PD is glyceraldehyde-3-phosphate dehydrogenase. (GPA)2 and (GPB)2 are dimers, and GPA-GPB is a heterodiraer. [Reproduced with permission from J. B. Stanbury, J. B. Wyngaarden, D. S. Fredrickson, et al. (Eds.), The Metabolic Basis of Inherited Disease, 5th ed. McGraw-Hill, New York, 1983.]...

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