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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: pdf
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
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