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Related Experiment Videos

Precipitation of soluble affinity complexes by a second affinity interaction: a model study.

C Senstad1, B Mattiasson

  • 1Department of Biotechnology, University of Lund, Sweden.

Biotechnology and Applied Biochemistry
|February 1, 1989
PubMed
Summary

Researchers purified lactate dehydrogenase using affinity precipitation. The enzyme bound to Blue Dextran and was co-precipitated with concanavalin A, offering a novel purification method.

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Area of Science:

  • Biochemistry
  • Protein Purification

Background:

  • Lactate dehydrogenase (LDH) is a crucial enzyme in cellular metabolism.
  • Efficient purification methods are essential for biochemical and diagnostic applications.

Purpose of the Study:

  • To develop and demonstrate a novel affinity precipitation technique for lactate dehydrogenase purification.

Main Methods:

  • Affinity precipitation utilizing Blue Dextran and concanavalin A.
  • Blue Dextran served as the affinity ligand for LDH.
  • Concanavalin A acted as a crosslinking agent to precipitate the enzyme-dextran complex.

Main Results:

  • Successful purification of lactate dehydrogenase was achieved through affinity precipitation.
  • The method effectively co-precipitated LDH bound to Blue Dextran using concanavalin A.

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  • Formation of large flocs facilitated the precipitation process.

    • Conclusions:

    • Affinity precipitation with Blue Dextran and concanavalin A is a viable method for lactate dehydrogenase purification.
    • This technique offers an efficient approach for isolating LDH.
    • The study highlights the utility of lectin-mediated precipitation in enzyme purification.