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. 1988 Feb;85(4):1057-9.
doi: 10.1073/pnas.85.4.1057.

Fibronectin as a carrier for the transglutaminase from human erythrocytes

L Lorand  1 , J E Dailey, P M Turner
Affiliations

Fibronectin as a carrier for the transglutaminase from human erythrocytes

L Lorand et al. Proc Natl Acad Sci U S A. 1988 Feb.

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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