Ishioka N, Sato J, Kurioka S
Division of Biochemistry, Jikei University School of Medicine, Tokyo, Japan.
Biochem Biophys Res Commun. 1994 Mar 30;199(3):1174-80. doi: 10.1006/bbrc.1994.1354.
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.