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Related Concept Videos

Size-Exclusion Chromatography01:08

Size-Exclusion Chromatography

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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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The stability and compatibility of column material with samples are crucial for efficient purification in chromatographic techniques. Various operating parameters such as pH, temperature, or solvent affect the packing of the column material, thereby determining the purification efficiency. The choice of column material also plays an essential role in deciding the operating parameters and can be modified based on the proteins that need to be purified.
Gel Filtration Chromatography
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Overview Of Cell Separation And Isolation01:20

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Cell separation was first achieved in 1964 by S. H. Seal, who separated large tumor cells from the smaller blood cells using filtration. Two years later, Pohl and Hawk performed experiments on how cells respond differently to a nonuniform electric field based on the cell type. Such observations were the inception of cell separation methods, which allow isolating a single cell type from a heterogeneous sample.
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Capillary Electrophoresis: Applications01:30

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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.
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Principles Of Column Chromatography01:13

Principles Of Column Chromatography

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The chromatography technique was first invented in 1901 by Michael S. Tswett, a Russian botanist, to separate plant pigments using organic solvents. Further, in 1941, Archer John Porter Martin and R. L. M. Synge modified the technique by packing silica gel into a column. A mixture of amino acids was then separated on the packed column using chloroform and water mixture as the mobile phase. This was the first report on column chromatography. At present, column chromatography is a widely used...
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SDS-PAGE01:27

SDS-PAGE

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Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
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Updated: Apr 28, 2026

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Separating proteins with activated carbon.

Matthew T Stone1, Mikhail Kozlov

  • 1EMD Millipore Corp., 80 Ashby Road, Bedford, Massachusetts 01730, United States.

Langmuir : the ACS Journal of Surfaces and Colloids
|June 6, 2014
PubMed
Summary
This summary is machine-generated.

Activated carbon effectively separates proteins by size and charge. Guidelines optimize impurity removal and protein recovery based on pH and isoelectric points for broad applicability.

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Area of Science:

  • Biochemistry
  • Separation Science
  • Materials Science

Background:

  • Activated carbon is a versatile adsorbent used in various separation processes.
  • Protein separation is crucial in biotechnology and pharmaceutical industries.
  • Understanding adsorption mechanisms is key to optimizing separation efficiency.

Purpose of the Study:

  • To establish guidelines for efficient protein separation using activated carbon.
  • To investigate the influence of pH and isoelectric point on protein adsorption and desorption.
  • To demonstrate the broad applicability of activated carbon for protein separation.

Main Methods:

  • Binding capacities of individual polymers and proteins were measured.
  • Three guidelines for protein separation were developed based on experimental data.
  • Activated carbon was tested for protein separation using static treatment and packed columns.
  • Three types of activated carbon were evaluated for their separation capabilities.

Main Results:

  • Activated carbon efficiently removes smaller protein impurities from larger proteins.
  • Optimal removal of impurities occurs at a pH near their isoelectric point (minimal charge).
  • Maximal recovery of small proteins from activated carbon is achieved at a pH away from their isoelectric point (maximal charge).

Conclusions:

  • The developed guidelines enable efficient separation and recovery of proteins using activated carbon.
  • Activated carbon demonstrates broad applicability for protein separation across different types and methods.
  • This method offers a practical approach for purifying protein mixtures.