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Related Concept Videos

Two-dimensional Gel Electrophoresis01:22

Two-dimensional Gel Electrophoresis

Two-dimensional gel electrophoresis is a high-resolution protein separation method first introduced by O' Farrell and Klose in 1975. This method involves protein separation by two dimensions, mass and charge, making it more accurate than one-dimensional gel electrophoresis.
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as  cells...
Ion-Exchange Chromatography01:09

Ion-Exchange Chromatography

Ion-exchange chromatography, or IEC, is a technique for separating ions based on their affinity for the stationary phase. The stationary phase is a cross-linked polymer resin with covalently attached ionic functional groups. The functional groups can be either positively charged (cation exchangers) or negatively charged (anion exchangers). A cation exchanger consists of a polymeric anion and active cations, while an anion exchanger is a polymeric cation with active anions. The choice of...
Capillary Electrophoresis: Applications01:30

Capillary Electrophoresis: Applications

Capillary electrophoretic separations offer various modes, each with unique applications. These modes include capillary zone electrophoresis, capillary gel electrophoresis, capillary array electrophoresis, capillary isoelectric focusing, capillary isotachophoresis, micellar electrokinetic chromatography, and capillary electrochromatography.
Capillary zone electrophoresis (CZE) separates ionic components based on their electrophoretic mobility. It has been used to separate proteins, amino acids,...
Centrifugation01:05

Centrifugation

Centrifugation is a separation technique based on differences in density or size. It is commonly used to separate solids from aqueous interferents. During centrifugation, the sample is placed in centrifugation tubes and spun at high angular velocity, which allows centrifugal force to act differentially on the different densities or masses of the components. After spinning, the supernatant liquid is decanted. Depending on the specific application, either the pellet or the supernatant is retained...
Detergent Purification of Membrane Proteins01:18

Detergent Purification of Membrane Proteins

Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...
Size-Exclusion Chromatography01:08

Size-Exclusion Chromatography

In size-exclusion chromatography (SEC), also known as molecular-exclusion or gel-permeation chromatography, molecules are separated based on their sizes. This technique is important for separating large molecules such as polymers and biomolecules. The two classes of micron-sized stationary phases encountered in SEC are silica particles and cross-linked polymer resin beads. Both materials are porous, but their pore sizes vary significantly.
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Cell Co-culture Patterning Using Aqueous Two-phase Systems
10:11

Cell Co-culture Patterning Using Aqueous Two-phase Systems

Published on: March 26, 2013

Aqueous two-phase systems for protein separation: a perspective.

Juan A Asenjo1, Barbara A Andrews

  • 1Centre for Biochemical Engineering and Biotechnology, Department of Chemical Engineering and Biotechnology, Institute for Cell Dynamics and Biotechnology: A Centre for Systems Biology, University of Chile, Beauchef 850, Santiago, Chile. juasenjo@ing.uchile.cl

Journal of Chromatography. A
|July 15, 2011
PubMed
Summary
This summary is machine-generated.

Aqueous two-phase systems (ATPS) effectively separate proteins by exploiting hydrophobicity. Protein partitioning depends on system properties, concentration, and bioaffinity, enabling industrial purification and virus separation.

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11:12

Organic Solvent-Based Protein Precipitation for Robust Proteome Purification Ahead of Mass Spectrometry

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Area of Science:

  • Biochemistry and Chemical Engineering
  • Separation Science
  • Biotechnology

Background:

  • Aqueous two-phase systems (ATPS) are versatile for protein separation and purification.
  • These systems are formed using polymers like polyethylene glycol (PEG) with salts or other polymers.
  • Protein partitioning in ATPS is influenced by protein surface properties and system characteristics.

Purpose of the Study:

  • To review the key factors governing protein partitioning in ATPS.
  • To highlight trends and mechanisms of protein separation using ATPS.
  • To discuss the practical applications and industrial relevance of ATPS for biomolecule purification.

Main Methods:

  • Analysis of factors influencing protein partitioning: hydrophobicity, charge, concentration, molecular weight, and bioaffinity.
  • Review of methods for measuring protein hydrophobicity relevant to ATPS.
  • Examination of partitioning behavior at varying protein concentrations, including precipitation phenomena.

Main Results:

  • Hydrophobicity is the primary determinant of protein partitioning in ATPS.
  • Protein charge has a minor effect in PEG/salt systems but is significant in PEG/dextran systems.
  • Partitioning behavior is concentration-dependent, with distinct regimes for true partitioning and high-concentration effects like precipitation.

Conclusions:

  • ATPS offer effective and scalable methods for protein purification, demonstrated by industrial applications.
  • Understanding partitioning trends, particularly hydrophobicity, is crucial for optimizing separation processes.
  • ATPS are also applicable for separating viruses and virus-like particles, broadening their utility.