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Characterization of the kinetics of neural cell adhesion molecule homophilic binding
Author(s) -
Moran Niamh,
Bock Elisabeth
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80998-0
Subject(s) - neural cell adhesion molecule , polyclonal antibodies , chemistry , kinetics , adhesion , cell adhesion , binding site , cell adhesion molecule , biophysics , receptor–ligand kinetics , microbiology and biotechnology , antibody , cell , biochemistry , biology , receptor , immunology , quantum mechanics , physics , organic chemistry
A solid‐phase assay has been developed for the investigation of the kinetics of neural cell adhesion molecule (NCAM) binding. Using this assay we can show that NCAM binds to itself in a time‐dependent and saturable manner. Binding constants ( K B values) of 6.9 × 10 −8 M and 1.23 × 10 −6 M, respectively, were obtained for adult and newborn rat NCAM homophilic binding. Binding is specifically inhibited by Fab′ fragments of polyclonal anti‐NCAM antibodies but is unaffected by heparin or chondroitin sulphate. This indicates that the NCAM homophilic binding site is separate from and independent of the heparin‐binding site and that a developmental modification, probably polysialation, gives rise to marked differences in the adhesive properties of NCAM.