Abstract
A neurite outgrowth molecule was purified from soluble fraction of bovine brain by reversed-phase column HPLC following concanavalin A (Con A)-affinity chromatography. This molecule was a 74kDa (named sGP74) and clearly reacted with the monoclonal antibody HNK-1. The amino acid sequences of N-terminal portion and peptides derived from trypsin digests of sGP74 were nearly identical to those of rat brain ankyrin-binding protein (ABGP186) that is a member of immunoglobulin superfamily with adhesive function. Our results suggest that sGP74 preserves multiple immunoglobulin-like domains and is released from an extracellular site of ABGP186.
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