Disulphide bonds are a requirement for adsorption of cephalosporins on the red cell membrane.
The authors studied the behavior of red cells (RBCs), treated with 2-aminoethylisothiouronium bromide (AET), against 100 serums containing cephalothin antibodies and 27 serums with cephapirin antibodies. None of the serums reacted with cephalosporin-coated RBCs that had been exposed previously to AET. The possibility of the Kell system acting as a receptor for cephalosporins was excluded. The authors discuss the significance of cysteine disulphide bonds and the tertiary or quaternary structure of red cell membrane proteins in the binding of cephalosporins to RBCs.
D000327:Adsorption; D000906:Antibodies / Q000276:immunology; D002511:Cephalosporins / Q000276:immunology / Q000378:metabolism*; D002512:Cephalothin / Q000276:immunology; D055598:Chemical Phenomena; D002621:Chemistry; D003298:Coombs Test; D003545:Cysteine / Q000502:physiology; D004347:Drug Interactions; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D006801:Humans; D013438:Sulfhydryl Compounds / Q000494:pharmacology*; D000338:beta-Aminoethyl Isothiourea / Q000494:pharmacology
D000906:Antibodies; D002511:Cephalosporins; D013438:Sulfhydryl Compounds; D000338:beta-Aminoethyl Isothiourea; D003545:Cysteine; D002512:Cephalothin