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

dc.contributor.authorBimanpalli, M V
dc.contributor.authorGhaswala, P S
dc.date.accessioned2015-07-27T05:24:08Z
dc.date.available2015-07-27T05:24:08Z
dc.date.issued1988-06
dc.description.abstractPrealbumin 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.en_US
dc.identifier.citationBimanpalli M V, Ghaswala P S. Isolation, purification and partial characterisation of prealbumin from cerebrospinal fluid. Journal of Biosciences. 1988 Jun; 13(2): 159-169.en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/160656
dc.language.isoenen_US
dc.source.urihttps://www.ias.ac.in/jarch/jbiosci/13/159-169.pdfen_US
dc.subjectPrealbuminen_US
dc.subjectprotein purificationen_US
dc.subjectgel electrophoresisen_US
dc.subjectgel filtrationen_US
dc.subjectImmunoelectrophoresisen_US
dc.subjectamino acid analysisen_US
dc.titleIsolation, purification and partial characterisation of prealbumin from cerebrospinal fluid.en_US
dc.typeArticleen_US
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