Crosslinking of membrane proteins during erythrocyte ageing.
Membrane proteins of bovine erythrocytes were crosslinked with cupric di(1,10-phenanthroline) and analysed by one-dimensional and two-dimensional SDS-polyacrylamide gel electrophoresis. An increase in crosslinking of the Band 3 protein and of spectrin was found with increasing erythrocyte age suggesting an increased aggregation of main membrane proteins in aged erythrocytes.
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Gaczyńska
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Bartosz
D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism; D002417:Cattle; D003432:Cross-Linking Reagents / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D004905:Erythrocyte Aging; D004910:Erythrocyte Membrane / Q000502:physiology*; D007700:Kinetics; D008565:Membrane Proteins / Q000097:blood* / Q000302:isolation & purification; D010618:Phenanthrolines / Q000494:pharmacology; D013049:Spectrin / Q000378:metabolism
D001457:Anion Exchange Protein 1, Erythrocyte; D003432:Cross-Linking Reagents; D008565:Membrane Proteins; D010618:Phenanthrolines; D013049:Spectrin; C014741:bis(1,10-phenanthroline)copper(2+) ion