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. 1991 Dec 1;88(23):10601–10604. doi: 10.1073/pnas.88.23.10601

Intramolecular crosslinking of monomeric fibrinogen by tissue transglutaminase.

S N Murthy 1, J Wilson 1, S L Guy 1, L Lorand 1
PMCID: PMC52977  PMID: 1683705

Abstract

In addition to generating polymeric products from human fibrinogen, human erythrocyte transglutaminase (protein-glutamine:amine gamma-glutamyltransferase, EC 2.3.2.13) was shown to catalyze the intramolecular reaction of crosslinking two of the constituent chains within monomeric fibrinogen itself. This internally fused protein derivative contains appreciable amounts of the N epsilon-(gamma-glutamyl)lysine bridge peptide and displays the A alpha.gamma hybrid chain pattern of crosslinking, characteristic for the actions of tissue transglutaminases on fibrinogen. Diagnostic analysis in pathological situations, where such enzymes might have escaped from cells into the plasma environment, should include a search for the internally crosslinked soluble fibrinogen monomer.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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