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Transglutaminases: purification and activity assays

B Wilhelm1, A Meinhardt, J Seitz

  • 1Department of Anatomy and Cell Biology, Philipps University, Marburg, Germany.

Journal of Chromatography. B, Biomedical Applications
|September 20, 1996
PubMed
Summary

This review summarizes methods for isolating transglutaminases (TGases), enzymes crucial for protein cross-linking. It details chromatographic and electrophoretic techniques for purifying these challenging proteins.

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Area of Science:

  • Biochemistry
  • Protein Chemistry

Background:

  • Transglutaminases (TGases) are a diverse protein family present in vertebrate tissues and fluids.
  • Various TGase types exist, including secretory, tissue, epidermal, keratinocyte, hemocyte, factor XIIIa, and erythrocyte TGase.
  • TGases are challenging to isolate due to their tendency to form irreversible aggregates under native conditions.

Purpose of the Study:

  • To review and summarize established isolation and purification procedures for different transglutaminase types.
  • To provide an overview of chromatographic and electrophoretic techniques applicable to TGase purification.
  • To describe established activity assays for TGases based on their enzymatic function.

Main Methods:

  • Chromatographic techniques: size-exclusion, ion-exchange, hydrophobic-interaction, affinity, and adsorption chromatography.

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  • Electrophoretic techniques: preparative isoelectric focusing, SDS-PAGE, and zone electrophoresis.
  • Enzymatic activity assays based on TGase's cross-linking function.

    • Main Results:

    • Detailed summary of isolation procedures for various TGase types.
    • Description of commonly used and alternative purification methods.
    • Overview of established TGase activity assays.

    Conclusions:

    • Effective isolation and purification of TGases are achievable through various chromatographic and electrophoretic methods.
    • Understanding these techniques is vital for studying TGase function and applications.
    • Established activity assays facilitate the characterization of purified TGases.