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- W2513632749 abstract "Complex formation between the human erythrocyte transglutaminase (protein-glutamine:amine y-glu- tamyltransferase, EC 2.3.2.13) and fibronectin or its fragments was examined by immunoanalytical procedures and by fluo- rescence polarization. A 42-kDa gelatin-binding structure, obtained from human plasma fibronectin by thermolytic di- gestion, showed as high an affinity for the cytosolic enzyme as the parent fibronectin chains themselves. A 21-kDa fragment comprising type I modules 8 and 9, the last two modules in the 42-kDa fragment, bound with an affinity 100-fold less than the 42-kDa fragment. Binding was remarkably specific and could be exploited for the affinity purification of transglutaminase directly from the hemoglobin-depleted erythrocyte lysate. In spite of the high affinity, it was possible to elute active enzyme from the 42-kDa fragment column with 0.25% monochloro- acetic acid. This solvent might have general applicability in other systems involving separation of tightly bound ligands. Plasma fibronectin is thought to play an important homeo- static role by acting as a scavenger for cytosolic transglu- taminases (TGs; protein-glutamine:amine y-glutamyltrans- ferase, EC 2.3.2.13). Such enzymes occur in many different cell types and could pose the danger of polymerizing proteins" @default.
- W2513632749 created "2016-09-16" @default.
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- W2513632749 date "2016-01-01" @default.
- W2513632749 modified "2023-10-17" @default.
- W2513632749 title "Affinity of human erythrocyte transglutaminase for a 42-kDa gelatin-binding fragment of human plasma fibronectin (collagen-binding domain/ELISA/fluorescence polarization/thermolytic fragment)" @default.
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