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http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/1360| Título : | An unusual triosephosphate isomerase from the early divergent eukaryote Giardia lamblia |
| Creador: | López Velázquez, Gabriel |
| Nivel de acceso: | Open access |
| Palabras clave : | Secuencia de Aminoácidos Cisteína - Analisis Citoplasma - Enzimología Electroforesis en Gel de Poliacrilamida Estabilidad de Enzimas Giardia lamblia - enzimología Amino Acid Sequence Cysteine - analysis Cytoplasm - enzymology Electrophoresis, Polyacrylamide Gel Enzyme Stability Giardia lamblia - enzymology Glucólisis giardiasis Proteína de purificación Estado de oligomerización Disulfuro Glycolysis Giardiasis Protein purifica-tion Oligomerization state Disulfides |
| Descripción : | Recombinant triosephosphate isomerase from the parasite Giardia lamblia (GlTIM) was characterized and immunolocalized. The enzyme is distributed uniformly throughout the cytoplasm. Size exclusion chromatography of the purified enzyme showed two peaks with molecular weights of 108 and 55 kDa. Under reducing conditions, only the 55-kDa protein was detected. In denaturing gel electrophoresis without dithiothreitol, the enzyme showed two bands with molecular weights of 28 and 50 kDa; with dithiotretitol, only the 28-kDa protein was observed. These data indicate that GlTIM may exist as a tetramer or a dimer and that, in the former, the two dimers are covalently linked by disulfide bonds. The kinetics of the dimer were similar to those of other TIMs. The tetramer exhibited half of the k cat of the dimer without changes in the Km. Studies on the thermal stability and the apparent association constants between monomers showed that the tetramer was slightly more stable than the dimer. This finding suggests the oligomerization is not related to enzyme thermostability as in Thermotoga maritima. Instead, it could be that oligomerization is related to the regulation of catalytic activity in different states of the life cycle of this mesophilic parasite. © 2004 Wiley-Liss, Inc. |
| Colaborador(es) u otros Autores: | Molina Ortiz D Cabrera N Hernández Alcántara G Peon Peralta J Yépez Mulia L Pérez Montfort R Reyes Vivas H. |
| Fecha de publicación : | 2004 |
| Tipo de publicación: | Artículo |
| Formato: | |
| Identificador del Recurso : | 10.1002/prot.20097 |
| Fuente: | Proteins: Structure, Function and Genetics 55(4):824 - 834 |
| URI : | http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/1360 |
| Idioma: | eng |
| Aparece en las colecciones: | Artículos |
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