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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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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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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...
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Two-dimensional Gel Electrophoresis

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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.
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Overview Of Cell Separation And Isolation01:20

Overview Of Cell Separation And Isolation

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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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The homogenate obtained after cell lysis contains various membrane-bound organelles that can be further separated into pure fractions by subcellular fractionation. These isolates are used to study specific cellular components, analyze localized protein activity, and are even employed in diagnostics. Fractionation is typically achieved using centrifugation methods, the most common being density-gradient and differential centrifugation.
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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

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Protein separation by sequential selective complex coacervation.

Jin Zhou1, Ying Cai1, Yuting Wan1

  • 1State-Key Laboratory of Chemical Engineering, and Shanghai Key Laboratory of Multiphase Materials Chemical Engineering, East China University of Science and Technology, 130 Meilong Road, 200237 Shanghai, People's Republic of China.

Journal of Colloid and Interface Science
|June 24, 2023
PubMed
Summary
This summary is machine-generated.

This study introduces a sequential coacervation method for purifying proteins like Bovine Serum Albumin (BSA) and Horseradish Peroxidase (HRP). The process efficiently separates proteins with different isoelectric points, offering a sustainable industrial solution.

Keywords:
Complex coacervationPolyelectrolytesProtein separationSelective complexation

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Area of Science:

  • Biochemistry
  • Materials Science
  • Chemical Engineering

Background:

  • Efficient isolation of specific proteins is crucial for food manufacturing and biomedical applications.
  • Purifying proteins from natural sources presents significant challenges.
  • Existing methods often struggle with selectivity and scalability.

Purpose of the Study:

  • To develop a sequential coacervation process for selective protein isolation and purification.
  • To separate Bovine Serum Albumin (BSA) and Horseradish Peroxidase (HRP) from a mixed solution.
  • To demonstrate a scalable and sustainable protein separation strategy.

Main Methods:

  • Utilized sequential complex coacervation triggered by polyelectrolytes (polyethyleneimine and poly(acrylic acid)).
  • Manipulated pH and ionic strength to achieve selective protein complexation.
  • Employed phase separation to isolate and purify target proteins (BSA and HRP).

Main Results:

  • Achieved 100% Horseradish Peroxidase (HRP) in the supernatant with 91% purity in the first step.
  • Recovered approximately 75% of Bovine Serum Albumin (BSA) with 99% purity in the second step.
  • Demonstrated selective protein separation based on differing isoelectric points (pIs).

Conclusions:

  • Sequential coacervation under controlled conditions enables selective protein purification.
  • The developed method is facile, sustainable, and shows potential for industrial-scale protein separation.
  • This approach offers an efficient alternative for obtaining pure proteins for various applications.