Fibronectin as a carrier for the transglutaminase from human erythrocytes.
AUTOR(ES)
Lorand, L
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=279700Documentos Relacionados
- Staining of the A antigen human erythrocytes.
- Pili as a mediator of the attachment of gonococci to human erythrocytes.
- Mammalian reticulocytes lose adhesion to fibronectin during maturation to erythrocytes.
- Glutathione transport by inside-out vesicles from human erythrocytes.
- Glycine transport in human erythrocytes.