Cross-linking of erythrocyte membrane proteins by periodate and intramembrane particle distribution.
Treatment of isolated human erythrocyte membranes at pH 7.4 with 0.1-0.5 mM-sodium periodate specifically cross-linked some of the spectrin polypeptides. Treatment with 2 mM-periodate resulted in complete cross-linking of spectrin and partial cross-linking of other polypeptides. The latter treatment also caused aggregation of the intramembrane particles made visible by freeze-fracturing. When membranes that had been treated with 2 mM-periodate were depleted of spectrin by treatment with 0.1 mM-EDTA, extensive aggregation of the intramembrane particles occurred.
D000596:Amino Acids / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000648:ultrastructure; D004912:Erythrocytes / Q000187:drug effects*; D006801:Humans; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000378:metabolism*; D010504:Periodic Acid / Q000494:pharmacology*; D013049:Spectrin / Q000378:metabolism*
D000596:Amino Acids; D008565:Membrane Proteins; D010504:Periodic Acid; D013049:Spectrin