Protein electropherograms

This protein or group of proteins is characterized as four to five bands on SDS—polyacrylamide gel electropherograms in the range from 58,(K)0 to 65,000, and by their ability to recycle with tubulin and stimulate microtubule assembly. [See pp. 33—37 of the review by Kirschner (1978) for an excellent overview of this protein and its properties]... 

Integration of the electropherogram for an antibody to quantify main protein species percent light chain and heavy chain (%LC and %HC) and minor species such as percent non-main and percent high molecular weight species (%non-main species and %HMW) is shown in Figure 5. Corrected peak areas were used for quantification. The % corrected peak area is defined as ... 

FIGURE 22 clEF electropherograms of a protein using different vendors of pi markers (aligned using the dominant antibody peak). 

Fig. 9 Electropherograms showing 3 nM fluorescently labeled 11-mer in the absence (A) and in the presence (B) of 0.7 /j,M SSB protein in the running buffer. The conditions used were as follows separation capillary, 35 cm, 20-/xm i.d. running buffer, 25 mM disodium tetraborate (pH 9.1) separation voltage, 25 kV excitation wavelength, 488 nm emission wavelength, 515 nm and temperature, 25 (1°C. Approximately 1 nL of sample solution was injected electrokinetically. The asterisk indicates the migration time of the solvent, The traces Iv and Ih, corresponding to vertically and horizontally polarized fluorescence intensities, respectively, are shown separated for clarity. (From Ref. 48.)...

Because the ability to dye one protein may differ from that of another in an electropherogram, an unknown protein mix should become stained by different methods. Some of the procedures can be done sequential in the same gel, e.g., additional Coomassie staining after silver staining. 

Figure 5. Presentation of the change in levels of several beef proteins identified by capillary electrophoresis (CE). Electropherograms are shown in the insert. Numbers refer to the identification or name assigned to each peak.

Figure 10. Capillary electropherogram of beef extract in the presence of liposomes and a free radical oxidation generator (FROG). Upper chromatogram is the initial unincubated protein profile while the lower profile is the protein profile after one hour incubation with the liposome + FROG system (adapted from 6).

Accessorial Proteins. In sodium dodecylsulfate gel electropherograms a few smaller protein components comprising less than 20 % of the total membrane protein migrate ahead of the main protein. Different migration patterns have been... 

Electropherogram of major proteins from a single erythrocyte. Peaks A, B, and C are carbonic anhydrase ( 7 amol), methemoglobin ( 5 amol), and hemoglobin A0 ( 450 amol), as identified from migration times relative to standards.3 Courtesy of Edward S. Yeung. 

Figure 4.5 NCE/ESI QTOF-MS and tandem MS electropherograms of DNA-binding domain of human TTAGGG repeat binding factor 2 (hTRF2 DBD) protein. (A) Mass electropherogram of hTRF2 DBD [M+ 5H]S+ ion at m/z 1509, and (B) top-down by CID MS/MS of ion corresponding to the peak number 5 at 10.88 min [8],...

Peptide mapping studies, generated by the cleavage of a protein into peptide fragments, must be highly reproducible and quantitative. Several electropherograms of protein digests have been obtained when chicken ovalbumin was cleaved by trypsin... 

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