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Research Papers
Bio/Technology  8, 543 - 546 (1990)
doi:10.1038/nbt0690-543

Characterization of Recombinant Factor XIIIa Produced in Saccharomyces cerevisiae

Ursula Rinas1, Bernhard Risse1, Rainer Jaenicke1, *, Michael Bröker2, Hermann E. Karges2, Hans A. Küpper2 & Gerd Zettlmeissl2

  1Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, D-8400 Regensburg, FRG.

  2Research Laboratories Behringwerke AG, P.O. Box 1140, D-3550 Marburg/Lahn, FRG.

  *Corresponding author.

Recombinant factor XIIIa (FXIIIa), produced in Saccharomyces cerevisiae, was recovered as a fully active cytosolic component and rigorously compared to natural F XIIIa from human placenta with respect to physicochemical and functional properties. Identical parameters were found in SDS polyacrylamide gel electrophoresis, analytical ultracentrifugation and HPLC gel filtration, and all spectral characteristics including derivative UV absorbance, fluorescence and circular dichroism were identical. Similarly, the interaction of both proteins with polyclonal antibodies directed against the entire FXIIIa or its N-terminal 4 kD activation peptide were identical. Furthermore, thrombin cleavage and fibrin cross-linking showed indistinguishable patterns. The only difference we observed was with respect to endgroup analysis. The recombinant protein is homogeneous, whereas placental FXIIIa shows multiple electrophoretic bands caused by microheterogeneity in the C-terminal part of the protein.

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