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Protein purification.

E P Lillehoj, V S Malik

    Advances in Biochemical Engineering/Biotechnology
    |January 1, 1989
    PubMed
    Summary
    This summary is machine-generated.

    This review covers essential protein purification and analysis techniques for both natural and recombinant proteins. It details strategies for isolation, including chromatography and electrophoresis, crucial for biochemical research.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Analytical Chemistry

    Background:

    • Protein purification and analysis are fundamental to understanding protein function and structure.
    • Advances in biotechnology have increased the demand for efficient methods to isolate and characterize proteins.

    Purpose of the Study:

    • To summarize recent developments in natural and recombinant protein purification and analysis.
    • To review basic strategies for protein isolation, considering protein characteristics, starting materials, and denaturants.

    Main Methods:

    • Initial steps: cell-free extracts, bulk precipitation, phase partition.
    • Chromatographic techniques: size exclusion, ion exchange, hydroxylapatite, reversed phase, hydrophobic interaction, affinity chromatography (low and high pressure).

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  • Electrophoretic techniques: SDS-PAGE, isotachophoresis, IEF, 2D gel electrophoresis for homogeneity analysis.

    • Main Results:

    • Comprehensive overview of protein purification strategies.
    • Detailed discussion of various chromatographic and electrophoretic methods.
    • Emphasis on analytical techniques for assessing protein purity.

    Conclusions:

    • Effective protein purification relies on strategic selection of methods based on protein properties.
    • A combination of chromatographic and electrophoretic techniques ensures successful isolation and analysis.
    • This monograph serves as a guide to current protein purification and analysis practices.