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Human Erythrocyte Membranes: Effect of Lipid Extraction on Binding of IgG (‘Warm’) Autoantibodies and Rh Isoantibodies 1
Author(s) -
LEDDY J. P.,
WHITTEMORE N. B.,
WEED R. I.
Publication year - 1970
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1970.tb01775.x
Subject(s) - autoantibody , glycoprotein , antibody , chemistry , antigen , isoantibodies , serology , membrane , microbiology and biotechnology , erythrocyte membrane , biochemistry , biology , immunology
. Solubilized membrane glycoprotein derived from human erythrocytes by extraction in aqueous butanol lost all detectable capacity to bind γG (‘warm’) autoantibodies, whether the latter exhibited ‘Rh‐related’ or undefined serologic specificities. The same membrane glycoprotein, previously shown to retain A, B and H antigenic activities, also displayed complete loss of binding capacity for anti‐D (Rh o ), anti‐C (rh′), anti‐E (rh″), anti‐c (hr′) and anti‐e (hr″) iso antibodies.