A SOLUBLE NEURITE OUTGROWTH MOLECULE IN BOVINE BRAIN

A neurite outgrowth molecule was purified from soluble fraction of bov ine brain by reversed-phase column HPLC following concanavalin A (Con A)-affinity chromatography. This molecule was a 74kDa (named sGP74) an d clearly reacted with the monoclonal antibody HNK-1. The amino acid s equences of N-terminal portion and peptides derived from trypsin diges ts of sGP74 were nearly identical to those of rat brain ankyrin-bindin g protein (ABGP186) that is a member of immunoglobulin superfamily wit h adhesive function. Our results suggest that sGP74 preserves multiple immunoglobulin-like domains and is released from an extracellular sit e of ABGP186. (C) 1994 Academic Press, Inc.