1958
DOI: 10.1021/j150566a005
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Electrophoretic and Titration Study of Bovine Plasma Albumin

Abstract: Electrophoretic mobilitiea for crystallized bovine plasma albumin in the pH range 1-11 at ionic strengths of 0.1, 0.05 and 0.01 and a protein concentration of 0.5 g./100 ml. have been determined. Titrations of the protein at ionic strengths of 0.1 and 0.01 have been carried out at 0°. The apparent heterogeneity of bovine plasma albumin is indicated in the electrophoresis results. The comparison of the mobility and titration data indicates an increase of the frictional coefficient in acid solution, in agreement… Show more

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Cited by 21 publications
(6 citation statements)
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“…these calculations was evaluated using an expression from Rodilosso (1984). The values of ue (Table 2) were in good agreement with available experimental data (Schlessinger, 1958; Norde and Lyklema, 1978). The variation in D" with NaCl concentration (values given in Table 2) was calculated from available theory for spherical solutes (Oshima et al, 1984; Van de Ven, 1989), with the value at very high ionic strength taken from available experimental data for BSA diffusion (Doherty and Benedek, 1974).…”
Section: Results and Analysissupporting
confidence: 74%
“…these calculations was evaluated using an expression from Rodilosso (1984). The values of ue (Table 2) were in good agreement with available experimental data (Schlessinger, 1958; Norde and Lyklema, 1978). The variation in D" with NaCl concentration (values given in Table 2) was calculated from available theory for spherical solutes (Oshima et al, 1984; Van de Ven, 1989), with the value at very high ionic strength taken from available experimental data for BSA diffusion (Doherty and Benedek, 1974).…”
Section: Results and Analysissupporting
confidence: 74%
“…The sample zone was 0.1 mL of a preparation of 10 pL of approximately 10' plaque-forming units (pfu/mL) of phages in 2 mL of the appropriate density gradient fraction. Figure 5 shows the mobility values of serum albumin from extrapolation to q,, (viscosity of the buffer solution at 0% sucrose concentration and ZONAL DENSITY GRADIENT ELECTROPHORESIS 201 4°C) compared to data obtained by Stenhagen (34) and Schlessinger (35). The comparison shows good agreement with the literature values.…”
Section: Methodssupporting
confidence: 75%
“…The idea of using electrophoresis to study ion binding is well-established. Many investigators have used the Tiselius moving boundary technique to measure protein electrophoretic mobility in different buffers. More recently, Douglas et al developed a free-flow electrophoresis cell to measure protein mobilities. However, both of these techniques require relatively large (typically microgram to milligram) quantities of protein and use complex analytical systems to evaluate the mobilities.…”
mentioning
confidence: 99%