Electrophoretic mobilities of proteins and protein mixtures
β Scribed by N.G. Douglas; A.A. Humffray; H.R.C. Pratt; G.W. Stevens
- Book ID
- 103010501
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 969 KB
- Volume
- 50
- Category
- Article
- ISSN
- 0009-2509
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstraet--Electrophoretic mobilities of bovine serum albumin (SA), haemoglobin (Hb) and ovalbumin (OA) have been determined by direct ultramicroscopic observation of the velocities of individual particles in a particle electrophoresis apparatus, and of SA and Hb in a free-flow apparatus of the type described independently by Hannig and by Strickler. Agreement between the results obtained by the two methods for SA and Hb o(,er wide pH ranges covering both sides of the respective isoelectric points was surprisingly good. Runs were also conducted in the free-flow cell in which SA was transported in buffer containing Hb, and vice versa; these showed clear evidence of interactions between the motions of the two proteins, as occurs in the parallel case of multicomponent diffusion, but the results could not be quantified in terms of the Maxwell-Stefan theory. Finally, the single protein data were compared with predictions made on the basis of the Debye-Huckel-Henry theory, and showed reasonable agreement.
π SIMILAR VOLUMES
The electrophoretic mobility of haemoglobin was measured in a novel membrane-electrophoresis cell and by electrophoretic light scattering. The effect of protein concentration was investigated at different ionic strengths in two different buffer systems. The results indicated that although the effect
Electrophoretic mobilities, \(\mu\), of nine proteins \(\left(M_{\mathrm{r}}\right.\) 14,200 to 70,000 ) in \(28 \mathrm{mM}\) Tris/47 \(\mathrm{mM}\) glycine buffer at \(\mathrm{pH} 8.77\) and \(5 \mathrm{~mm}\) ionic strength were measured by laser Doppler velocimetry and correlated to ratios of c