Gel electrophoretic patterns

Fig. 3. Sodium dodecyl sulfate—polyacrylamide gel electrophoretic pattern for molecular weight standards (lane 1) water-extractable proteins of defatted soybean meal (lane 2) purified IIS (glycinin) (lane 3) and purified 7S (P-conglycinin) (lane 4) where the numbers represent mol wt x 10. The gel was mn in the presence of 2-mercaptoethanol, resulting in the cleavage of the disulfide bond linking the acidic (A bands) and basic (B bands) polypeptides of the...

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.

The stability of these foams is improved only with samples heated for certain time intervals, for example, 0 to 45 min at 50 and 75OC, and 0 to 30 min and 60 to 75 min at lOOOC. At lOO C and 60 to 75 min, major changes in proteins are occurring, as shown on the gel electrophoretic patterns. 

Fla. 11. Starch gel electrophoretic patterns of red cell hemolyzates with the six phenotypes representing homozygosity and heterozygosity for the three common genes at the acid phosphatase locus, P, Pb, and Pc. From Giblett (79). 

DEAE-cellulose column was further purified on Sephadex G-200 but resisted all efforts at crystallization. Figure 14 (4) shows the polyacrylamide gel electrophoretic pattern of crude rat liver extract with two bands, the resolution of these bands by DEAE-cellulose, and the crystalline peak I preparation. The crystalline enzyme had an approximate molecular weight of 100,000 estimated by sucrose density gradient... 

Figure 4. Poly acrylamide-disc gel electrophoretic patterns obtained for forms of CBH I from Trichoderma (2). The protein samples applied to these gels were, from left to right 20 fxg CBH I (A), 15 fig CBH I (B), 33 jig CBH I (C), and 40 fig CBH 1 (D). Forms A, B, and C were purified from a commercial T. viride cellulose preparation and Form D was purified from a culture of T. reesei QM 9123 grown on purified cellulose.

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).

Figure 6. Gel electrophoretic patterns for the preparations of anti-gal and anti-lac antibodies (1)...

Figure 7. Electrofocusing pattern (top panel) and gel electrophoretic patterns (bottom panel) for the anti-gal isoantibodies (20 j...

Effect of Environmental Factors on Starch Gel Electrophoretic Patterns of Human Erythrocyte Acid Phosphatase... 

Fig. 16. Starch-gel electrophoretic patterns of acetylated ovotransferrins. (A, B, and C) Iron ovotransferrin acetylated for 20, 10, and 5 minutes, respectively (D, E, and F) ovotransferrin acetylated for 20, 10, and 5 minutes, respectively (G) control ovotransferrin. Samples were the same as employed in expt A, Table I acetylation with acetic anhydride as described in text. (Biochemistry 4, 998 [1965]).

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 8. Starch-gel electrophoretic patterns of incubated infertile eggs. Egg whites were all white Leghorn containing globulin At. Eggs were incubated at 37°C for 6 days or stored at 2°C for 6 days (controls). Letters refer to hen (22).

Figure 9. Disc-gel electrophoretic patterns of 11S soybean globulin stored in a frozen or concentrated state, (a), original solution (b), after 2 days storage in a frozen state at —5°C (c), after the addition of 0.01 M mercaptoethanol (ME) to solution (b) (d), after 2 days of storage in a concentrated state (unfrozen) and (e), after the addition of 0.01M mercaptoethanol to solution (d) (lO).

Fig. 27.—A and B Electrophoresis and agar diffusion of isoantibodies in gels 4 and 10 (of Fig. 26B). C Sodium dodecyl sulfate gel-electrophoretic patterns for the anti-lactose isoantibodies (Ab), light (L) and heavy (H) chains and dissociated isoantibodies (gels 6, 7, 8, 9, and 10 of Fig. 26B). (Reprinted with permission from Journal of Protein Chemistry, Volume 6, J. H. Pazur, M. E. Tay, B. A. Pazur, and F. J. Miskiel, pp. 387-399, copyright 1987 Journal of Protein Chemistry.)...

Fig. 18. Starch gel electrophoretic patterns of lyophilized gastric juice from 4 normal subjects. A, 5 mg of lyophilate B, 20 mg of lyophilate. Numerals refer to individual subjects. Electrophoresis in borate buffer at pH 8.6 for 5 hours. These electrophoretic patterns were selected to illustrate the variation in cathodal staining (amido black lOB stain). From Jeffries et al. (J4).

The starch gel electrophoretic patterns obtained by Hopkinson (Hll) and his associates (H14) and subsequently by others in Harris group (H2) and elsewhere in the world (G3, K2) are shown in Fig. 1. Initial studies by Hopkinson et al. (H13) on 139 randomly selected English males and females revealed the existence of five patterns with the following frequencies in the population type A, 10.1% type BA, 46% type B, 34.5% type CA, 36% type CB, 5.8%. On the basis of genetic considerations, they predicted the existence of a sixth type, C. Lai (Ll) and his associates (L2) obtained a different distribution in a Brazilian population, but reported evidence for the existence of the type C electrophoretic pattern. Additional studies by Hopkinson (Hll) modified the incidences of the patterns slightly A, 13% BA, 43% B, 36% CA, 3% CB, 5% C, 0.016%. 

Disc gel electrophoretic patterns show large differences between human serum, the two non-Antarctic fish sera and the two Antarctic fish sera (Fig. 2). Large differences were also noted on comparison of patterns of electrophoretic separations of human serum and the serum of T. borchgrevinki by molecular exclusion on Sephadex G-200 (Fig. 3). These differences were reflected in the amounts of proteins in the different fractions for these separations of D. mawsoni and the king salmon sera (Table III). The AFGP were found in fractions III from the sera of both T. borchgrevinki and D. mawsoni. Since fractions III also contained the albumins, it is evident that the albumin contents of these sera were much lower than those of human serum. Their sera... 

The sequential purification of T. borchgrevinki serum on a DEAE-cellulose ion-exchange column and a QAE-Sephadex A-25 column is seen in Figs. 4 and 5. Slab-gel electrophoretic patterns of the mixture of active AFGP components 1-5 and of the three main active... 

The SDS-gel electrophoretic pattern of tropomyosin showed two bands, designated a and /8, around 35,000 Da (Cummins and Perry, 1973). The ratio of the two subunits varied from tissue to tissue mostly a subunit in fast skeletal muscle, equimolar a and )8 subunits in slow skeletal muscle, and exclusively a subunit in cardiac muscle (Bronson and Schachat, 1982). The tropomyosin molecule consists of aa or ajS dimers. A )8/8 molecule produced in vitro showed the same Ca -sensitizing action as that of aj8- or aa-tropomyosin (Cummins and Perry, 1973). Hence physiologically both a and /3 subunits are identical. 

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.]...

Figure I. Reproduction of slab-gel electrophoretic pattern representing all of the major antifreeze glycoproteins present in the T. borchgrevinki and B. saida. The numbers on top refer to the components present in T. borchgrevinki (10).

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