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Erythrocyte Endogenous Proteinase Activity during Blood Bank Storage
Author(s) -
Angelis V.,
Matteis M. C.,
Orazi B. M.,
Santarossa L.,
Toffola L. Della,
Raineri A.,
Vettore L.
Publication year - 1990
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1990.tb05012.x
Subject(s) - proteolysis , red blood cell , endogeny , lysis , calpain , sodium dodecyl sulfate , gel electrophoresis , red cell , biochemistry , membrane protein , polyacrylamide gel electrophoresis , blood cell , biology , proteolytic enzymes , chemistry , microbiology and biotechnology , enzyme , membrane , immunology , medicine
. We studied proteolytic alterations of membrane proteins in ghosts derived from human red blood cells, preserved up to 35 days in the liquid state either as whole blood or with additive solution. The study was carried out by performing sodium dodecyl sulfate polyacrylamide gel electrophoresis of stromal proteins from erythrocytes, either previously treated with proteinase inhibitors or previously incubated in conditions promoting proteolysis. To differentiate the effect of erythrocyte from granulocyte proteinases, the investigation was also carried out in leukocyte‐free red cell preparations. The results show: (1) the effects of endogenous proteinases on membrane proteins derived from red cells stored under blood bank conditions; (2) a decrease of proteolytic effects in ghosts derived from red cells which have been submitted to a longer storage; (3) a relevant influence of the red cell resuspending medium before lysis on the time‐dependent onset and exhaustion of proteolysis in ghosts. The presence of increased proteolysis in ghosts could be regarded as a marker of molecular lesions induced in red cells by storage under blood bank conditions.