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Disulphide bonds are a requirement for adsorption of cephalosporins on the red cell membrane
Author(s) -
DuranSuarez J. R.,
MartinVega C.,
Massuet L.,
Ribera A.,
Pujol M.
Publication year - 1987
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.1537-2995.1987.27387235636.x
Subject(s) - cephalosporin , red cell , chemistry , antibody , cell membrane , membrane , bromide , biochemistry , medicine , immunology , antibiotics , organic chemistry
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.