Premium
Red Cell Membrane Protein Changes Caused by Freezing and the Mechanism of Cryoprotection by Glycerol
Author(s) -
Ballas S. K.
Publication year - 1981
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1981.21281178158.x
Subject(s) - membrane , glycerol , chemistry , band 3 , chromatography , elution , red blood cell , tonicity , biochemistry , sodium , cell membrane , gel electrophoresis , polyacrylamide gel electrophoresis , electrophoresis , enzyme , membrane protein , organic chemistry
Membranes isolated from frozen‐thawed erythrocytes and analyzed by polyacrylamide gel electrophoresis in sodium dodecyl sulfate have significantly decreased band six, which is the glycolytic enzyme, glyceraldehyde 3‐phosphate dehydrogenase. The total membrane protein and sialic acid contents of these membranes are also significantly decreased. The red blood cell membrane protein abnormality is reproduced by suspending membranes in NaCl solutions of increasing molarity. Glycerol prevents the elution of band six in NaCl solutions less than 0.2 M and ameliorates it in solutions of higher ionic strength. When intact cells are suspended in hypertonic salt solution, there is no elution of band six, indicating that exposure of the inner surface of the membrane to toxic concentrations of solutes results in this elution. The data indicate that freezing with its associated hypertonicity induces a specific membrane change which is ameliorated by the addition of glycerol.