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https://saber.ucv.ve/jspui/handle/10872/1718Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Ponte-Sucre, Alicia | - |
| dc.contributor.author | Ramirez, Jose Luis | - |
| dc.date.accessioned | 2012-08-28T19:31:36Z | - |
| dc.date.available | 2012-08-28T19:31:36Z | - |
| dc.date.issued | 2012-08-28 | - |
| dc.identifier.issn | 0716-9760 | - |
| dc.identifier.uri | http://hdl.handle.net/10872/1718 | - |
| dc.description.abstract | The enzyme pyruvate kinase of Leishmania mexicana amazonensis presents two forms with different kinetic properties and behavior for the heterotrophic activator fructose 2,6 bisphosphate. Pyruvate kinase 1, which is isolated as a tetramer, is inhibited by this metabolite. The second activity, Pyruvate kinase 2, is activated by fructose 2,6 bisphosphate, which promotes the monomer-tetramer conversion of this enzyme. | es_VE |
| dc.description.sponsorship | European Community, Consejo de Desarrollo Cientifico y Humanistico de la UCV | es_VE |
| dc.language.iso | en_US | es_VE |
| dc.relation.ispartofseries | Biological Research;26: 131-134, 1993. | - |
| dc.subject | Fructose 2,6 bisphosphate | es_VE |
| dc.subject | Pyruvate kinase | es_VE |
| dc.subject | Leishmania | es_VE |
| dc.title | Fructose 2,6 bisphosphate promotes the monomer-tetramer conservation of Leishmania mexicana amazonensis pyruvate kinase type two. | es_VE |
| dc.type | Article | es_VE |
| Appears in Collections: | Artículos Publicados | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Ponte Sucre y Ramirez, 1993.jpg | 1.13 MB | JPEG | View/Open |
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