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. 1981 Sep 29;670(2):139-45.
doi: 10.1016/0005-2795(81)90001-5.

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

B S Hong, P F Davison

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

B S Hong et al. Biochim Biophys Acta. .

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 electrohporesis and isoelectric focusing. The peptide from several species showed immunocrossreaction with rabbit antibody to intact glial fibrillary acidic protein. The peptide has a pI value of 5.32. The amino acid sequence of 28 residues from the amino terminus of the calf peptide has been determined.

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