Abstract
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.
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Abbreviations
- CSF:
-
Cerebrospinal fluid
- M r :
-
molecular weight
- BSA:
-
bovine serum albumin
- PAGE:
-
Polyacrylamide disc gel electrophoresis
- SDS:
-
sodium dodecyl sulphate
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Part of the Ph. D. thesis submitted by the first author.
An erratum for this article can be found at http://dx.doi.org/10.1007/BF02712161
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Bimanpalli, M.V., Ghaswala, P.S. Isolation, purification and partial characterisation of prealbumin from cerebrospinal fluid. J Biosci 13, 159–169 (1988). https://doi.org/10.1007/BF02903098
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DOI: https://doi.org/10.1007/BF02903098