Isolation, purification and partial characterisation of prealbumin from cerebrospinal fluid.

Prealbumin from human cerebrospinal fluid was purified using a combination of ammonium sulphate precipitation, phenol precipitation, Polyacrylamide disc gel electrophoresis and gel filtration on Sephadex G-100. The homogeneity of the purified protein was established by Polyacrylamide gel electrophoresis and Immunoelectrophoresis. On the basis of its molecular weight (55,000), amino acid composition, electrophoretic mobility and immunological cross-reactivity, the prealbumin from cerebrospinal fluid showed complete identity with serum prealbumin. The cerebrospinal fluid prealbumin levels in various neurological disorders may have a diagnostic significance.