| Revue: | Memorias do Instituto Oswaldo Cruz |
| Base de datos: | PERIÓDICA |
| Número de sistema: | 000420041 |
| ISSN: | 0074-0276 |
| Autores: | Contreras-Rodríguez, Luis Ernesto1 Marin-Mogollon, Catherin Yizet1 Sánchez-Mejía, Lina Marcela1 Ramírez-Hernández, María Helena1 |
| Instituciones: | 1Universidad Nacional de Colombia, Facultad de Ciencias, Bogotá. Colombia |
| Año: | 2018 |
| Volumen: | 113 |
| Número: | 9 |
| País: | Brasil |
| Idioma: | Inglés |
| Tipo de documento: | Artículo |
| Enfoque: | Experimental, aplicado |
| Resumen en inglés | ABSTRACT The biochemical pathways involved in nicotinamide adenine dinucleotide (NAD) biosynthesis converge at the enzymatic step catalysed by nicotinamide mononucleotide adenylyltransferase (NMNAT, EC: 2.7.7.1). The majority of NMNATs are assembled into homo-oligomeric states that comprise 2-6 subunits. Recently, the NMNAT of Plasmodium falciparum (PfNMNAT) has been identified as a pharmacological target. The enzymatic characterisation, cellular location, and tertiary structure of the PfNMNAT protein have been reported. Nonetheless, its quaternary structure remains to be explored. The present study describes the oligomeric assembly of the 6 x His-PfNMNAT recombinant protein using immobilised metal affinity chromatography coupled with size exclusion chromatography (SEC) and native protein electrophoresis combined with Ferguson plot graphing. These chromatographic approaches resulted in the elution of an active monomer from the SEC column, whereas the Ferguson plot indicated a dimeric assembly of the 6 x His-PfNMNAT protein |
| Disciplinas: | Medicina |
| Palabras clave: | Microbiología, Bioquímica, Biosíntesis, Nicotinamida mononucleótido adeniltransferasa, Oligomeros, Ensamblaje, Plasmodium falciparum |
| Keyword: | Microbiology, Biochemistry, Biosynthesis, Nicotinamide mononucleotide adenylyltransferase, Oligomers, Assembly, Plasmodium falciparum |
| Texte intégral: | Texto completo (Ver HTML) |
