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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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1437-4315
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Volume 390, Issue 12

Issues

Coagulation factor XIII variants with altered thrombin activation rates

Mette Dahl Andersen
  • Biopharmaceutical Research Unit, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Måløv, Denmark
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Marianne Kjalke
  • Biopharmaceutical Research Unit, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Måløv, Denmark
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Susanne Bang
  • Biopharmaceutical Research Unit, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Måløv, Denmark
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Inger Lautrup-Larsen / Peter Becker
  • Biopharmaceutical Research Unit, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Måløv, Denmark
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Asser Sloth Andersen / Ole Hvilsted Olsen
  • Biopharmaceutical Research Unit, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Måløv, Denmark
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Henning R. Stennicke
  • Biopharmaceutical Research Unit, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Måløv, Denmark
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2009-10-06 | DOI: https://doi.org/10.1515/BC.2009.142

Abstract

Coagulation factor XIII (FXIII) is activated by thrombin and catalyses crosslinking between fibrin monomers thereby providing mechanical strength to the fibrin network. V34L is a common FXIII-A polymorphism found in the activation peptide. FXIII-A V34L is activated faster by thrombin and provides formation of a tighter clot at fibrinogen concentrations in the low end of the physiological range. FXIII-A variants with potentially increased activation rates were generated. Introduction of an optimal thrombin cleavage site, V34L+V35T, increased the activation rate 7.6-fold and facilitated the formation of a fibrin network more resistant to fibrinolysis than obtained with wt FXIII-A. In contrast, introduction of fragments of fibrinopeptide A into the activation peptide resulted in severely impaired activation rates.

Keywords: enzyme activation; factor XIII; factor XIII activation peptide; thrombin

About the article

Corresponding author


Received: 2009-04-23

Accepted: 2009-08-17

Published Online: 2009-10-06

Published in Print: 2009-12-01


Citation Information: Biological Chemistry, Volume 390, Issue 12, Pages 1279–1283, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2009.142.

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