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DC Field | Value | Language |
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dc.contributor.author | Candra, Krishna Purnawan | |
dc.contributor.author | Roggentin, Peter | |
dc.contributor.author | Schauer, Roland | |
dc.date.accessioned | 2011-03-28T06:50:05Z | |
dc.date.available | 2011-03-28T06:50:05Z | |
dc.date.issued | 2005 | |
dc.identifier.issn | 0854-8587 | - |
dc.identifier.uri | http://repository.ipb.ac.id/handle/123456789/43379 | |
dc.description.abstract | Using sialyl-methylumbelliferyl α-glycoside as substrate, sialidase in horse liver was detected as a membrane-bound enzyme. A yield of about 50% of sialidase activity was found in supernatant when solubilized in 0.1 M sodium-phosphate buffer pH 5.5, containing 0.15 M NaCl, 0.25 M sucrose, and 0.5% Triton X-100. Sialidase in the solubilisate could be activated by incubating in acidic pH at 37 oC. Incubation of this solubilized enzyme at 37 oC for 1.5 h at pH 5.0 led to 10% increase of activity and to the precipitation of about 50% of contaminating protein. Using cation-exchange chromatography on S-Sepharose FF and affinity chromatography on p-aminophenyl oxamic acid-agarose following solubilization and activation, about 6% of total sialidase activity was recovered with the purification factor of about 500. The pH and temperature optimum were measured at pH 4.3 and between 37-45 oC, respectively. Neu5Ac2en was a strong inhibitor, while p-aminophenyl oxamic acid had only a weak inhibitory effect. | en |
dc.publisher | IPB (Bogor Agricultural University) | |
dc.relation.ispartofseries | Vol 12;No 3 | - |
dc.title | Solubilization, Activation and Partial Purification of a Sialidase from Horse Liver | en |
dc.title.alternative | HAYATI Journal of Biosciences Vol. 12 No.3 Tahun 2005 | en |
Appears in Collections: | Hayati Journal of Biosciences |
Files in This Item:
File | Description | Size | Format | |
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Krishna Purnawan Candra.pdf | e-Journal | 296.51 kB | Adobe PDF | View/Open |
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