Isolation and characterization of a soluble, immunoactive peptide of glial fibrillary acidic protein

Abstract

A soluble immunoactive peptide with a molecular weight of 16 000 was isolated and purified from the cyanogen bromide digest of the insoluble 50 000 dalton glial fibrillary acidic protein by Sephacryl S-200 gel filtration followed by DEAE-Bio-gel A chromatography. The homogeneity of the peptide was established by SDS-polyacrylamide gel electrophoresis and isoelectric focusing. The peptide from several species showed immunocrossreaction with rabbit antibody to intact glial fibrillary acidic protein. The peptide has a $\text{p}\text{I}$ value of 5.32. The amino acid sequence of 28 residues from the amino terminus of the calf peptide has been determined.