Isolation, purification and partial characterisation of prealbumin from cerebrospinal fluid.
dc.contributor.author | Bimanpalli, M V | |
dc.contributor.author | Ghaswala, P S | |
dc.date.accessioned | 2015-07-27T05:24:08Z | |
dc.date.available | 2015-07-27T05:24:08Z | |
dc.date.issued | 1988-06 | |
dc.description.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. | en_US |
dc.identifier.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. | en_US |
dc.identifier.uri | https://imsear.searo.who.int/handle/123456789/160656 | |
dc.language.iso | en | en_US |
dc.source.uri | https://www.ias.ac.in/jarch/jbiosci/13/159-169.pdf | en_US |
dc.subject | Prealbumin | en_US |
dc.subject | protein purification | en_US |
dc.subject | gel electrophoresis | en_US |
dc.subject | gel filtration | en_US |
dc.subject | Immunoelectrophoresis | en_US |
dc.subject | amino acid analysis | en_US |
dc.title | Isolation, purification and partial characterisation of prealbumin from cerebrospinal fluid. | en_US |
dc.type | Article | en_US |