Entrapment of protein protease inhibitors in red blood cells
Falcioni, G.; Gabbianelli, R.; Santroni, A.M.; Concetti, A.; Zolla, L.; Brunori, M.
Biotechnology and Applied Biochemistry 16(3): 269-274
1992
ISSN/ISBN: 0885-4513 PMID: 1282323 Document Number: 400993
Aprotinin and alpha 1-proteinase inhibitor have been encapsulated in human red blood cells (RBC) by a dialysis technique that involves transient hypotonic haemolysis followed by isotonic resealing. Both protease inhibitors can be encapsulated to a considerable extent. These molecules are released only by haemolysis of the cells and that excludes the possibility of using loaded erythrocytes for a slow release of the inhibitor(s) in the blood stream. However, the stability of the two inhibitors, the evidence for the binding of aprotinin to RBC components, and the results showing inhibition of endogenous proteolytic activity indicate that the inhibitors may be valuable in blocking, at least partially, undesired intraerythrocytic proteolytic reactions.