[Specific properties and primary structure of BASP1 protein, initially detected in neuronal axonal terminals].

The BASP1 protein is one of the acidic (pI 4.3-4.6) acid-soluble brain proteins; it is predominant in growth cones and presynaptic regions of neurons. This group also includes GAP-43/B-50 neuronal protein. However, primary structures of BASP1 and GAP-43/B-50 are different. Hydrophobicity of BASP1 protein is due to N-terminal myristic acid residue. BASP1 molecules purified from various animal species possess significant regions of homology; however, polyclonal antibodies raised against BASP1 from various species were species-specific. Hence, BASP1 molecules of various animals species include specific antigenic determinants located outside of the homology regions. Apart from brain, BASP1 was detected in several other tissues including lymphoid organs (spleen, thymus), kidney, and testis. Physico-chemical characteristics of brain BASP1 (myristoylation, pI, and isoforms) were identical with the proteins from other tissues. This suggests that BASP1 can have similar functions in various tissues.