A preparative isoelectric focusing (IEF) method was applied to separate skim milk proteins using the Rotofor device in a pH 3-10 gradient containing 4 M urealI % triton X-I 00. Each ofthe 20 fractions obtainedfrom the Rotofor device was then analyzed by polyacrylamide gel electrophoresis (PAGE). Both ureaPAGE and SDS-PAGE were used to separate purified caseins and skim milk resulting in compara...

Separation of milligram amounts of heparin oligosaccharides ranging in degree of polymerization from 4 to 32 is achieved within 6h using continuous elution polyacrylamide gel electrophoresis (CE-PAGE) on commercially available equipment. The purity and structural integrity of CE-PAGE-separated oligosaccharides are confirmed by strong anion exchange high-pressure liquid chromatography, electrosp...

Protein expression is a powerful technique to study the functional role of proteins both in vivo and in vitro. Various systems have been established to produce proteins in milligram quantities; however, the purification of many expressed proteins commonly results in trace amounts. We report on an improved method for the isolation of apolipoprotein A-I (apoA-I) using the Model 491 Prep Cell (Bio...

Here we describe a reliable method for purifying large amounts of RNA of any sequence and length with comparable efficiency and resolution of gel electrophoresis and with capacity approaching that of column chromatography. The RNA mixture of interest is separated on a cylindrical denaturing polyacrylamide gel, eluted by a peristaltic pump, detected by a UV-vis detector, and collected by a fract...

The alpha-2 macroglobulins from human serum and plasma were isolated by Bio-Gel P-300 and A5m gel filtration. The material showed a single peak on sedimentation velocity ultracentrifugation, a mol wt of 650,000 by sedimentation equilibrium ultracentrifugation, and a major precipitin arc in the alpha-2 macroglobulin region by immunoelectrophoresis against whole human serum. Two bands were observ...

The P700 chlorophyll a-protein was purified by preparative sodium dodecyl sulfate (SDS) gel electrophoresis from SDS-solubilized barley (Hordewm vulgare L., cv Himalaya) chloroplast membranes. After elution from the gel in the presence of 0.05 to 0.1% Triton X-100, the recovered protein had a chlorophyll/P70. ratio of 50 to 60/1 and contained no chlorophyll b or cytochromes. Analysis of the pol...

Aim: Despite intensive research during the last decade, it remains challenging to prepare extracellular vesicles (EVs) of high purity, especially from primary body liquids or protein-rich conditioned media. For now, time-consuming combinations at least two orthogonal methods, e.g., density and size separation, are required enrich EVs often expense processing time. Therefore, novel technologies ...