PMID: 6159283Jan 1, 1980Paper

Protein changes of the erythrocyte membrane during blood preservation

Folia haematologica : internationales Magazin für klinische und morphologische Blutforschung
D StibenzG Geyer

Abstract

The present study was conducted on erythrocytes banked in ACD-AG medium for 1, 21, or 42 days at 4 degrees C. Erythrocyte membrane proteins were analysed by means of SDS-polyacrylamide gel electrophoresis in relation to the action of beta-mercaptoethanol. Under banking conditions proteins of the erythrocyte membrane formed 380 000--420 000 daltons aggregates, presumably heterodimers of spectrin I and II, and very high molecular weight aggregates (MG > 600 000 daltons). Part of the aggregated proteins were cross-linked by disulfide bridges, which are subject of the reduction by beta-mercaptoethanol. The nonreducible components were considered an irreversible alteration of the erythrocyte membrane. Many samples of banked erythrocytes exhibited an increase of protein band II.3 (MG = 185 000 daltons) and band IV.2 (MG = 72 000 daltons). The amount of protein band VI (GAPDH) was shown to depend on both banking time and conditions of haemolysis. A modified hypotonic haemolysis with an additional intermediate alkaline incubation of ghosts resulted in a considerable decline of protein band VI of banked erythrocytes. Substraterich incubation of banked erythrocytes, which raised the ATP level well above normal, could only partially resto...Continue Reading

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