Isolation, purification and partial characterisation of prealbumin from cerebrospinal fluid.
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Date
1988-06
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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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Keywords
Prealbumin, protein purification, gel electrophoresis, gel filtration, Immunoelectrophoresis, amino acid analysis
Citation
Bimanpalli M V, Ghaswala P S. Isolation, purification and partial characterisation of prealbumin from cerebrospinal fluid. Journal of Biosciences. 1988 Jun; 13(2): 159-169.