Results 291 to 300 of about 66,610 (320)

Amphoteric, isoelectric immobiline membranes for preparative isoelectric focusing

Journal of Biochemical and Biophysical Methods, 1987
Amphoteric, isoelectric agarose membranes, as devised by Martin and Hampson [Martin, A.J.P. and Hampson, F. (1978) J. Chromatogr. 159, 101-110], are found unsuitable for blocking electroendosmosis in multi-compartment electrolysers during preparative isoelectric focusing, due to the poor and highly unpredictable incorporation of carboxyls and amino ...
P, Wenger, M, de Zuanni, P, Javet, C, Gelfi, P G, Righetti   +4 more
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Isoelectric focusing without ampholyte

Biochemical and Biophysical Research Communications, 1979
Summary We have studied the electrophoretic mobility of proteins in polyacrylamide gels when ampholyte and buffer were excluded from the system. We found, using a weak acid and base as anolyte and catholyte respectively, that a pH gradient was generated in the gel, and that proteins focused as sharp bands.
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Divergent flow isoelectric focusing

ELECTROPHORESIS, 2008
AbstractContinuous‐flow isoelectric focusing (IEF) has the potential to be an important method in proteome analysis. The current devices do not fully use the advantages of IEF, because they do not utilize all its important features including changes in background conductivity during the focusing.
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Isoelectric focusing in layers of granulated gels II. Preparative isoelectric focusing

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975
A method for preparative isoelectric focusing of 0.1-10 g amounts of proteins is described. For anticonvective stabilization of the pH gradient, layers of granulated gels (E.G. Sephadex or Bio-Gel) of variable length, width and thickness were used either on glass plates or in troughs.
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Isoelectric focusing in polyacrylamide gels

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
From many viewpoints, isoelectric focusing (IEF) represents a major advance in methodology for high-resolution separation of proteins and other amphoteric macromolecules. IEF is essentially an equilibrium method for segregating amphoteric molecules by electrophoresis in stable pH gradients according to their isoelectric points (pI).
P, Righetti, J W, Drysdale
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Two‐dimensional gel isoelectric focusing

ELECTROPHORESIS, 2005
AbstractTwo‐dimensional gel isoelectric focusing (2‐D gel IEF) is presented as the combination of the same separation method used consecutively in two directions of the same gel. In this new method, after completion of IEF process in the first dimension the gel was cut into the separate strips, each containing selected analytes together with the ...
Miroslava, Stastná, Karel, Slais
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Capillary isoelectric focusing

2013
Capillary isoelectric focusing (CIEF) is a widespread technique for the analysis of peptides and proteins in biological samples. CIEF is used to separate mixtures of compounds on the basis of differences in their isoelectric point. Aspects of sample preparation, capillary selection, zone mobilization procedures as well as various detection modes used ...
Bujak, Renata, Daghir, Emilia
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Preparative isoelectric focusing in agarose

Analytical Biochemistry, 1981
Abstract The use of agarose gels as supporting media for flat-bed preparative isoelectric focusing was applied to the fractionation of serum proteins in the pH range 3.5–6, and red cell hemolysates in the pH range 3–8. The agarose gels are easy to prepare, give linear pH gradients, and do not appear to produce molecular sieving effects.
C, Chapuis-Cellier, P, Arnaud
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Preparative Isoelectric Focusing

Separation and Purification Methods, 1975
Abstract Electrophoretic mobility has been used for years as a basis for separation and characterization of proteins. The resolving power of conventional electrophoresis is limited, and the characterization by mobility is not unique because of the dependence of the protein mobilities on the pH and ionic strength of the buffers.
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[35] Isoelectric focusing

1990
Publisher Summary Isoelectric focusing (IEF) is a technique that was developed to separate proteins on the basis of differences in their isoelectric pH value, termed “pI values.” It is used for both the analysis and preparative isolation of proteins. IEF is an electrophoretic method in which amphoteric molecules are separated as they migrate through ...
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