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Fibronectin as a carrier for the transglutaminase from human erythrocytes.

Authors
  • Lorand, L
  • Dailey, J E
  • Turner, P M
Type
Published Article
Journal
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Publication Date
Feb 01, 1988
Volume
85
Issue
4
Pages
1057–1059
Identifiers
PMID: 2893381
Source
Medline
License
Unknown

Abstract

Nondenaturing electrophoresis was used to demonstrate that, immediately upon exposure to plasma, the transglutaminase (protein-glutamine:amine gamma-glutamyltransferase, EC 2.3.2.13) from erythrocytes undergoes a significant shift in mobility. The plasma effect shows saturable characteristics and depends entirely on the presence of fibronectin in plasma, indicative of complex formation between this protein and transglutaminase. The results suggest a specific carrier function for fibronectin that might be of physiological importance in determining the fate of a tissue transglutaminase accidentally discharged into plasma.

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