Isolation, Purification, and Characterization of an Acidic Protein in the Cerebrospinal Fluid of Central Nervous System Disease

Abstract

Proteins from 21 cerebrospinal fluid (CSF) samples (14 derived from neurological cases and 7 from normal individuals) and 15 serum samples (11 from neurological cases and 4 from normal individuals) were analyzed by two-dimensional electrophoresis. Protein mapping revealed a very acidic protein (Ac-P) at about pH 3.5 in the 71% of CSF samples from neurological cases. However, no serum sample contained Ac-P. Ac-P was isolated and purified, and determined to be a glycoprotein containing a large amount of carbohydrate, with molecular weight 42, 000 and isoelectric point 2.7-3.3. The amino acid composition of Ac-P was consistent with α₁-acid glycoprotein (AGP), and Ac-P was responsive to a commercial anti-AGP antiserum in the radial immunodiffusion test.
 The known polymorphism of AGP suggests some differences in physicochemical properties such as molecular weight and isoelectric point between AGP in serum and in CSF. Quantitative analysis of Ac-P (AGP) and total protein levels in CSF showed a partial interdependence. Ac-P may be a useful marker for detecting a pathological conditions of the central nervous system.