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SN Gitel, VM Medina and S Wessler
Protein-heparin complexes, prepared by a water-soluble carbodiimide
coupling technique, were used to produce anti-heparin antibodies in
rabbits. Antiserums that recognized carbodiimide-treated heparin, but not
untreated heparin, were obtained. Carbodiimide-treated heparan sulfate
exhibited 10% to 20% cross-reactivity compared with a similarly treated
heparin, whereas there was no cross-reactivity with five other
carbodiimide-treated mucopolysaccharides. 3H-1-ethyl-3-(3-
trimethylammoniumpropyl) carbodiimide iodide was used to demonstrate that
carbodiimide forms a stable adduct with heparin and other
mucopolysaccharides. Using an antibody fraction that eluted from 1-
ethyl-3-(3-trimethylammoniumpropyl) carbodiimide iodide-treated heparin-
Sepharose with 2 mol/L KI, it was demonstrated that, for the antibody
population studied, the addition of one carbodiimide per heparin molecule
resulted in complete epitope expression without loss of anticoagulant
activity. The addition of up to eight additional carbodiimide molecules to
heparin did not increase the extent of epitope formation, although
anticoagulant activity was lost. Except for heparan sulfate, the addition
of radiolabeled carbodiimide to other mucopolysaccharides did not result in
epitope formation. These data demonstrate that antibodies to an epitope
derived from heparin can be formed, that the epitope is fully expressed
while anticoagulant activity is present, and that the antibody is
specifically directed against an altered portion of the polysaccharide.
This article has been cited by other articles:
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| Copyright © 1985 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
