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Demonstration of immunochemical identity between the nerve growth factor‐inducible large external (NILE) glycoprotein and the cell adhesion molecule L1.
Author(s) -
Bock E.,
RichterLandsberg C.,
Faissner A.,
Schachner M.
Publication year - 1985
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1985.tb04001.x
Subject(s) - biology , glycoprotein , identity (music) , cell adhesion molecule , nerve growth factor , adhesion , microbiology and biotechnology , membrane glycoproteins , biochemistry , receptor , chemistry , physics , organic chemistry , acoustics
The nerve growth factor‐inducible large external (NILE) glycoprotein and the neural cell adhesion molecule L1 were shown to be immunochemically identical. Immunoprecipitation with L1 and NILE antibodies of [3H]fucose‐labeled material from culture supernatants and detergent extracts of NGF‐treated rat PC12 pheochromocytoma cells yielded comigrating bands by SDS‐PAGE. NILE antibodies reacted with immunopurified L1 antigen, but not with N‐CAM and other L2 epitope‐bearing glycoproteins from adult mouse brain. Finally, by sequential immunoprecipitation from detergent extracts of [35S]methionine‐labeled early post‐natal cerebellar cell cultures or [3H]fucose‐labeled NGF‐treated PC12 cells, all immunoreactivity for NILE antibody could be removed by pre‐clearing with L1 antibody and vice versa.