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Electropherograms protein standards

Figure 8. Electropherogram of six protein standards obtained by capillary zone electrophoresis. The standards are A sperm whale myoglobin B horse myoglobin C human carbonic anhydrase D bovine carbonic anhydrase E 13-lactoglobulin B ... Figure 8. Electropherogram of six protein standards obtained by capillary zone electrophoresis. The standards are A sperm whale myoglobin B horse myoglobin C human carbonic anhydrase D bovine carbonic anhydrase E 13-lactoglobulin B ...
Figure 11. Electropherogram of protein standards run in an untreated fused silica capillary, in pH 8.24 tricine buffer. Figure 11. Electropherogram of protein standards run in an untreated fused silica capillary, in pH 8.24 tricine buffer.
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. [Pg.107]

While all of these devices used normal zone electrophoresis separation techniques, isoelectric focusing (IEF) methods on microchips have also been interfaced with ESI-MS for high-resolution separations of proteins [37], Figure 5 shows the electropherogram and corresponding mass spectra generated by this device. For on-chip sample preconcentration before separation, a polarityswitching technique was employed to achieve subnanomolar detection limits for many peptide standards [38],... [Pg.439]

An off-line approach that is simple and useful for peptide/protein sequencing using 5-10 picomoles of material has been demonstrated. Peptide and protein samples were first separated by capillary electrophoresis. Selected peaks were fraction collected and analyzed by both nano-electrospray mass spectrometry and Edman sequencing. A standard peptide mixture, a tryptic-digested protein and intact proteins were used to illustrate this method. Successful fraction collection of each component required reproducible electropherograms, the ability to automatically switch the outlet buffer vessel and the ability to maintain electrophoretic integrity while eluting a peak of interest into a small outlet buffer... [Pg.45]

FIGURE 30.6 Typical electropherogram of proteins in fresh milk. (1) fS-lactoglobulin, (2) bovine serum albumin, (3) a-lactalbumin, (4) conalbumin (added internal standard), (5) a-casein and (6) f(-casein (From Vallejo-Cordoba, B. J. Cap. Elec., 4, 219,1997. With permission.)... [Pg.889]

Fig. 1 The electropherogram from normal serum sample by CE. Running conditions Fused silica capillary, 25 xm I.D. x 27 cm detection at 214 nm applied potential, 10 kV with Beckman Coulter proprietary running buffer. Each peak is labeled with the protein, which has been identified by both spiking and immunosubtraction methods. Two peaks without label are internal standards. Fig. 1 The electropherogram from normal serum sample by CE. Running conditions Fused silica capillary, 25 xm I.D. x 27 cm detection at 214 nm applied potential, 10 kV with Beckman Coulter proprietary running buffer. Each peak is labeled with the protein, which has been identified by both spiking and immunosubtraction methods. Two peaks without label are internal standards.

See other pages where Electropherograms protein standards is mentioned: [Pg.1406]    [Pg.203]    [Pg.9]    [Pg.378]    [Pg.181]    [Pg.286]    [Pg.111]    [Pg.870]    [Pg.92]    [Pg.278]    [Pg.351]    [Pg.437]   
See also in sourсe #XX -- [ Pg.18 , Pg.193 ]




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