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Related Experiment Videos

Transgenically produced human antithrombin: structural and functional comparison to human plasma-derived antithrombin

T Edmunds1, S M Van Patten, J Pollock

  • 1Cell and Protein Therapeutics Department, Genzyme Corp, and Genzyme Transgenics Corp, Framingham, MA 01701-9322, USA.

Blood
|June 17, 1998
PubMed
Summary
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Recombinant human antithrombin (rhAT) from goat milk showed identical activity to plasma-derived AT (phAT) but a higher heparin affinity. Structural analysis revealed rhAT differs from phAT primarily in glycosylation patterns.

Area of Science:

  • Biotechnology
  • Biochemistry
  • Protein Engineering

Background:

  • Human antithrombin (AT) is a crucial anticoagulant protein.
  • Plasma-derived AT (phAT) is used therapeutically but has limitations.
  • Recombinant protein production offers an alternative source.

Purpose of the Study:

  • To characterize recombinant human antithrombin (rhAT) produced in transgenic goat milk.
  • To compare the structural and functional properties of rhAT with phAT.
  • To investigate the basis for any observed differences in heparin binding affinity.

Main Methods:

  • Purification of rhAT to >99% purity.
  • In vitro thrombin inhibition assay to assess specific activity.
  • Comparative analyses using RP-HPLC, CD, FACE, amino acid sequencing, and LC/MS peptide mapping.

Related Experiment Videos

  • Detailed glycan analysis of both rhAT and phAT.

    • Main Results:

    • rhAT exhibited specific activity identical to phAT.
    • rhAT demonstrated a fourfold higher affinity for heparin compared to phAT.
    • Structural analysis revealed rhAT and phAT are identical except for glycosylation.
    • rhAT contained oligomannose structures at Asn 155, unlike phAT.
    • rhAT showed differences in sialylation and fucosylation compared to phAT.

    Conclusions:

    • rhAT is structurally similar to phAT, with key differences in glycosylation.
    • The altered glycosylation, particularly oligomannose structures and sialylation, likely accounts for rhAT's increased heparin affinity.
    • rhAT represents a potentially valuable therapeutic alternative to phAT.